UA71551C2 - Formation of peptide/lipid vesicles and complexes through co-lyophilization of peptides - Google Patents

Formation of peptide/lipid vesicles and complexes through co-lyophilization of peptides Download PDF

Info

Publication number: UA71551C2
Authority: UA; Ukraine
Prior art keywords: lipid; peptide; item; specified; solution
Prior art date: 1997-10-02

Application number

UA2000042492A

Other languages

English (en)

Ukrainian (uk)

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1997-10-02

Filing date

1998-09-28

Publication date

2004-12-15

1998-09-28 Application filed filed Critical

2004-12-15 Publication of UA71551C2 publication Critical patent/UA71551C2/uk

Links

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230000015572 biosynthetic process Effects 0.000 title claims abstract description 19
239000000203 mixture Substances 0.000 claims abstract description 46
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 20
239000003599 detergent Substances 0.000 claims abstract description 15
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OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 claims description 51
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HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 claims description 18
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YAWNFGAHEUCLNJ-UHFFFAOYSA-N [B].OB(O)O Chemical compound [B].OB(O)O YAWNFGAHEUCLNJ-UHFFFAOYSA-N 0.000 description 1
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AWUCVROLDVIAJX-UHFFFAOYSA-N alpha-glycerophosphate Natural products OCC(O)COP(O)(O)=O AWUCVROLDVIAJX-UHFFFAOYSA-N 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
208000011454 apolipoprotein A-I deficiency Diseases 0.000 description 1
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GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 1
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KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
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OGGXGZAMXPVRFZ-UHFFFAOYSA-M dimethylarsinate Chemical compound C[As](C)([O-])=O OGGXGZAMXPVRFZ-UHFFFAOYSA-M 0.000 description 1
229960005160 dimyristoylphosphatidylglycerol Drugs 0.000 description 1
FRKBLBQTSTUKOV-UHFFFAOYSA-N diphosphatidyl glycerol Natural products OP(O)(=O)OCC(OP(O)(O)=O)COP(O)(O)=O FRKBLBQTSTUKOV-UHFFFAOYSA-N 0.000 description 1
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
230000006806 disease prevention Effects 0.000 description 1
208000035475 disorder Diseases 0.000 description 1
239000006185 dispersion Substances 0.000 description 1
BPHQZTVXXXJVHI-AJQTZOPKSA-N ditetradecanoyl phosphatidylglycerol Chemical compound CCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(=O)OC[C@@H](O)CO)OC(=O)CCCCCCCCCCCCC BPHQZTVXXXJVHI-AJQTZOPKSA-N 0.000 description 1
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239000003480 eluent Substances 0.000 description 1
238000005538 encapsulation Methods 0.000 description 1
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230000002255 enzymatic effect Effects 0.000 description 1
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230000008014 freezing Effects 0.000 description 1
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239000007789 gas Substances 0.000 description 1
239000007792 gaseous phase Substances 0.000 description 1
238000002523 gelfiltration Methods 0.000 description 1
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150000002433 hydrophilic molecules Chemical class 0.000 description 1
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230000003993 interaction Effects 0.000 description 1
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239000008101 lactose Substances 0.000 description 1
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239000002953 phosphate buffered saline Substances 0.000 description 1
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Classifications

- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/10—Dispersions; Emulsions
- A61K9/127—Liposomes
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/14—Particulate form, e.g. powders, Processes for size reducing of pure drugs or the resulting products, Pure drug nanoparticles
- A61K9/19—Particulate form, e.g. powders, Processes for size reducing of pure drugs or the resulting products, Pure drug nanoparticles lyophilised, i.e. freeze-dried, solutions or dispersions
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/62—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being a protein, peptide or polyamino acid
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/10—Dispersions; Emulsions
- A61K9/127—Liposomes
- A61K9/1275—Lipoproteins; Chylomicrons; Artificial HDL, LDL, VLDL, protein-free species thereof; Precursors thereof
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/10—Dispersions; Emulsions
- A61K9/127—Liposomes
- A61K9/1277—Processes for preparing; Proliposomes
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/775—Apolipopeptides
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/10—Dispersions; Emulsions
- A61K9/107—Emulsions ; Emulsion preconcentrates; Micelles
- A61K9/1075—Microemulsions or submicron emulsions; Preconcentrates or solids thereof; Micelles, e.g. made of phospholipids or block copolymers

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Medicinal Chemistry (AREA)
General Health & Medical Sciences (AREA)
Pharmacology & Pharmacy (AREA)
Animal Behavior & Ethology (AREA)
Public Health (AREA)
Veterinary Medicine (AREA)
Epidemiology (AREA)
Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Organic Chemistry (AREA)
Dispersion Chemistry (AREA)
Zoology (AREA)
Gastroenterology & Hepatology (AREA)
Immunology (AREA)
Toxicology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
Genetics & Genomics (AREA)
Molecular Biology (AREA)
Marine Sciences & Fisheries (AREA)
Diabetes (AREA)
Hematology (AREA)
Obesity (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Medicinal Preparation (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

UA2000042492A 1997-10-02 1998-09-28 Formation of peptide/lipid vesicles and complexes through co-lyophilization of peptides UA71551C2 (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US08/942,597 US6287590B1 (en)	1997-10-02	1997-10-02	Peptide/lipid complex formation by co-lyophilization
PCT/US1998/020330 WO1999017740A1 (en)	1997-10-02	1998-09-28	Peptide/lipid complex formation by co-lyophilization

Publications (1)

Publication Number	Publication Date
UA71551C2 true UA71551C2 (en)	2004-12-15

Family

ID=25478329

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
UA2000042492A UA71551C2 (en)	1997-10-02	1998-09-28	Formation of peptide/lipid vesicles and complexes through co-lyophilization of peptides

Country Status (20)

Country	Link
US (4)	US6287590B1 (no)
EP (2)	EP1019025B1 (no)
JP (1)	JP2001522781A (no)
KR (1)	KR100588241B1 (no)
CN (1)	CN100415210C (no)
AT (1)	ATE260644T1 (no)
AU (2)	AU749344B2 (no)
CA (1)	CA2305704C (no)
DE (1)	DE69822176T2 (no)
DK (1)	DK1019025T3 (no)
ES (1)	ES2217591T3 (no)
HU (1)	HUP0003930A3 (no)
IL (1)	IL135322A (no)
NO (1)	NO329155B1 (no)
NZ (1)	NZ503721A (no)
PL (1)	PL196579B1 (no)
PT (1)	PT1019025E (no)
RU (1)	RU2224506C2 (no)
UA (1)	UA71551C2 (no)
WO (1)	WO1999017740A1 (no)

Families Citing this family (71)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5746223A (en) *	1996-10-11	1998-05-05	Williams; Kevin Jon	Method of forcing the reverse transport of cholesterol from a body part to the liver while avoiding harmful disruptions of hepatic cholesterol homeostasis
US6004925A (en) *	1997-09-29	1999-12-21	J. L. Dasseux	Apolipoprotein A-I agonists and their use to treat dyslipidemic disorders
US6287590B1 (en)	1997-10-02	2001-09-11	Esperion Therapeutics, Inc.	Peptide/lipid complex formation by co-lyophilization
DE19954843C2 (de) *	1999-11-09	2003-11-20	Novosom Ag	Verfahren zur Verkapselung von Proteinen oder Peptiden in Liposomen, mit dem Verfahren hergestellte Liposomen und deren Verwendung
US6514523B1 (en)	2000-02-14	2003-02-04	Ottawa Heart Institute Research Corporation	Carrier particles for drug delivery and process for preparation
GB0121171D0 (en) *	2001-08-31	2001-10-24	Glaxosmithkline Biolog Sa	Vaccine
US7199102B2 (en) *	2000-08-24	2007-04-03	The Regents Of The University Of California	Orally administered peptides synergize statin activity
US7166578B2 (en)	2000-08-24	2007-01-23	The Regents Of The University Of California	Orally administered peptides synergize statin activity
US7723303B2 (en) *	2000-08-24	2010-05-25	The Regents Of The University Of California	Peptides and peptide mimetics to treat pathologies characterized by an inflammatory response
US8568766B2 (en)	2000-08-24	2013-10-29	Gattadahalli M. Anantharamaiah	Peptides and peptide mimetics to treat pathologies associated with eye disease
US7144862B2 (en) *	2000-08-24	2006-12-05	The Regents Of The University Of California	Orally administered peptides to ameliorate atherosclerosis
US6664230B1 (en) *	2000-08-24	2003-12-16	The Regents Of The University Of California	Orally administered peptides to ameliorate atherosclerosis
US7148197B2 (en) *	2000-08-24	2006-12-12	The Regents Of The University Of California	Orally administered small peptides synergize statin activity
EP1427436B1 (en)	2001-08-23	2008-07-02	Westgate Biological Limited	Use of milk serum apoproteins in the prophylaxis or treatment of microbial or viral infection
US20030229062A1 (en) *	2001-12-07	2003-12-11	The Regents Of The University Of California	Treatments for age-related macular degeneration (AMD)
US7470659B2 (en) *	2001-12-07	2008-12-30	The Regents Of The University Of California	Methods to increase reverse cholesterol transport in the retinal pigment epithelium (RPE) and Bruch's membrane (BM)
JP2005511713A (ja) *	2001-12-07	2005-04-28	ザ・リージェンツ・オブ・ザ・ユニバーシティー・オブ・カリフォルニア	加齢性黄斑変性についての処置
US6930085B2 (en) *	2002-04-05	2005-08-16	The Regents Of The University Of California	G-type peptides to ameliorate atherosclerosis
US20040009216A1 (en) *	2002-04-05	2004-01-15	Rodrigueza Wendi V.	Compositions and methods for dosing liposomes of certain sizes to treat or prevent disease
NL1020962C2 (nl) *	2002-06-28	2003-12-30	Tno	Therapie en prognose/monitoring bij sepsis en septische shock.
US10517883B2 (en)	2003-06-27	2019-12-31	Zuli Holdings Ltd.	Method of treating acute myocardial infarction
US20060051407A1 (en) *	2003-06-27	2006-03-09	Yoram Richter	Method of treating ischemia-reperfusion injury
PE20050438A1 (es) *	2003-10-20	2005-06-14	Esperion Therapeutics Inc	Formulas farmaceuticas, metodos y regimenes de dosificacion para el tratamiento y la prevencion de sindromes coronarios agudos
WO2005084642A1 (en) *	2004-01-28	2005-09-15	Biodelivery Sciences International, Inc.	Apoprotein cochleate compositions
JP4617458B2 (ja) *	2004-02-10	2011-01-26	財団法人ヒューマンサイエンス振興財団	中空糸透析カラムを利用したリポソームの製造方法
SE0401942D0 (sv) *	2004-07-28	2004-07-28	Lipopeptide Ab	New antimicrobial peptide complexes
CN101065137A (zh) *	2004-09-16	2007-10-31	加利福尼亚大学董事会	用于改善动脉粥样硬化和其它病变的g型多肽和其它剂
US7582312B2 (en) *	2004-11-15	2009-09-01	Discovery Laboratories, Inc.	Methods to produce lung surfactant formulations via lyophilization and formulations and uses thereof
US7464012B2 (en) *	2004-12-10	2008-12-09	L'air Liquide, Societe Anonyme A Directoire Et Conseil De Surveillance Pour L'etude Et L'exploitation Des Procedes Georges Claude	Simplified process simulator
RU2414236C2 (ru)	2004-12-06	2011-03-20	Зе Риджентс Оф Зи Юнивесити Оф Кэлифонье	Способ улучшения структуры и/или функций артериол
EP1866036A2 (en) *	2005-03-16	2007-12-19	Procyte Corporation	Methods and compositions for preventing and treating aging or photodamaged skin
US8206750B2 (en)	2005-03-24	2012-06-26	Cerenis Therapeutics Holding S.A.	Charged lipoprotein complexes and their uses
US20080293639A1 (en) *	2005-04-29	2008-11-27	The Regents Of The University Of California	Peptides and peptide mimetics to treat pathologies characterized by an inflammatory response
MX2007013430A (es) *	2005-04-29	2008-03-19	Univ California	Peptidos y peptidos mimeticos para tratar patologias caracterizadas por una respuesta inflamatoria.
US20070254832A1 (en) *	2006-02-17	2007-11-01	Pressler Milton L	Methods for the treatment of macular degeneration and related eye conditions
US8163699B2 (en) *	2006-06-01	2012-04-24	Montreal Heart Institute	Method for the treatment of valvular disease
EP2041174A2 (en) *	2006-06-16	2009-04-01	Lipid Sciences, Inc.	Novel peptides that promote lipid efflux
US20080227686A1 (en) *	2006-06-16	2008-09-18	Lipid Sciences, Inc.	Novel Peptides that Promote Lipid Efflux
US20080206142A1 (en) *	2006-06-16	2008-08-28	Lipid Sciences, Inc.	Novel Peptides That Promote Lipid Efflux
AU2007284801A1 (en)	2006-08-08	2008-02-21	The Regents Of The University Of Californina	Salicylanilides enhance oral delivery of therapeutic peptides
WO2008039843A2 (en) *	2006-09-26	2008-04-03	Lipid Sciences, Inc.	Novel peptides that promote lipid efflux
PL2081551T3 (pl) *	2006-10-06	2013-06-28	Scil Tech Gmbh	Wytworzenie wysuszonego rekonstytuowanego pęcherzyka do zastosowania farmaceutycznego
KR100817024B1 (ko)	2006-11-09	2008-03-26	재단법인 목암생명공학연구소	핵산 또는 약물을 간에 특이적으로 전달하는 복합체 및이를 포함하는 약학적 조성물
EP2173370B1 (en) *	2007-06-27	2015-10-21	The Board of Trustees of the Leland Stanford Junior University	Oligopeptide tyrosinase inhibitors and uses thereof
JP5568008B2 (ja) *	2007-06-27	2014-08-06	ザボードオブトラスティーズオブザレランドスタンフォードジュニアユニバーシティー	ペプチドチロシナーゼインヒビターおよびその使用
US8557767B2 (en)	2007-08-28	2013-10-15	Uab Research Foundation	Synthetic apolipoprotein E mimicking polypeptides and methods of use
JP2010538005A (ja)	2007-08-28	2010-12-09	ユーエービーリサーチファウンデーション	合成アポリポ蛋白質ｅ模倣ポリペプチドおよび使用方法
EP2389189A4 (en)	2009-01-23	2012-12-19	Inst Cardiologie Montreal	METHOD FOR PREVENTING AND TREATING DIASTOLIC DYSFUNCTION USING APOLIPOPROTEIN-A1 MIMETIC PEPTIDE / PHOSPHOLIPID COMPLEX (APOA1)
RU2532222C2 (ru)	2009-02-16	2014-10-27	Серенис Терапьютикс Холдинг С.А,	Миметики аполипопротеина а-i
WO2010095912A2 (ko) *	2009-02-23	2010-08-26	성균관대학교 산학협력단	난용성 약물 나노복합체의 제조방법
WO2011002258A2 (ko) *	2009-07-02	2011-01-06	한양대학교 산학협력단	아르기닌 기제 양친성 펩티드 마이셀
US10894098B2 (en)	2012-04-09	2021-01-19	Signablok, Inc.	Methods and compositions for targeted imaging
US20130137628A1 (en)	2010-05-11	2013-05-30	Esperion Therapeutics, Inc.	Dimeric Oxidation-Resistant Apolipoprotein A1 Variants
BR112013004397A2 (pt)	2010-08-30	2017-06-27	Hoffmann La Roche	método para produzir uma partícula de lipídio, a partícula de lipídio em si e seu uso
PL2767546T3 (pl)	2011-02-07	2019-04-30	Cerenis Therapeutics Holding Sa	Kompleksy lipoproteinowe i ich wytwarzanie oraz ich zastosowania
RU2457864C1 (ru) *	2011-07-28	2012-08-10	Общество с ограниченной ответственностью "Научно-производственная компания "ФАРМАСОФТ" (ООО "НПК "ФАРМАСОФТ")	Гель, обладающий противовоспалительным, иммунотропным, противоаллергическим и ранозаживляющим действием
US9993427B2 (en)	2013-03-14	2018-06-12	Biorest Ltd.	Liposome formulation and manufacture
WO2014144708A1 (en)	2013-03-15	2014-09-18	The Regents Of The University Of California	Peptides having reduced toxicity that stimulate cholesterol efflux
CN103860470A (zh) *	2014-03-05	2014-06-18	贵州中泰生物科技有限公司	一种口服高密度脂蛋白脂质体的制备方法
US20150316566A1 (en)	2014-05-02	2015-11-05	Cerenis Therapeutics Holding Sa	Hdl therapy markers
BR112017001860A2 (pt)	2014-07-31	2018-02-27	Uab Research Foundation	peptídeo sintético, composição farmacêutica, métodos, regime de dosagem, e, anticorpo monoclonal
WO2016068160A1 (ja) *	2014-10-30	2016-05-06	Ｄｅｌｔａ－ＦｌｙＰｈａｒｍａ株式会社	局所投与用リポプレックスの新規製造方法及び該リポプレックスを使用する抗腫瘍剤
WO2016154542A2 (en)	2015-03-25	2016-09-29	The Regents Of The University Of Michigan	Compositions and methods for treating cardiovascular related disorders
US20160346221A1 (en)	2015-06-01	2016-12-01	Autotelic Llc	Phospholipid-coated therapeutic agent nanoparticles and related methods
CA2991655A1 (en)	2015-07-10	2017-01-19	Peptinovo Biopharma, Llc	Formulations for improving the efficacy of hydrophobic drugs
EP3490579A1 (en)	2016-07-27	2019-06-05	Hartis-Pharma SA	Therapeutic combinations to treat red blood cell disorders
WO2018042576A1 (ja) *	2016-08-31	2018-03-08	キユーピー株式会社	卵黄リン脂質組成物およびその製造方法、ならびに該卵黄リン脂質組成物を用いた脂肪乳剤およびリポ化製剤
KR102039661B1 (ko)	2017-07-28	2019-11-01	경북대학교 산학협력단	HDL-ApoM-S1P를 유효성분으로 포함하는 퇴행성뇌질환의 예방 또는 치료용 약학적 조성물
WO2019030574A1 (en) *	2017-08-10	2019-02-14	Cerenis Therapeutics Holding	CARGOMÈRES
CN111249451B (zh) *	2020-01-20	2022-11-04	成都医学院	一种糖脂类抗原注射液及其制备方法
CN112034175A (zh) *	2020-04-03	2020-12-04	苏州艾可瑞斯生物科技有限公司	一种ApoA-II、ApoC-II检测混合质控品及其制备方法

Family Cites Families (17)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CH621479A5 (no)	1977-08-05	1981-02-13	Battelle Memorial Institute
CA1173360A (en)	1979-06-22	1984-08-28	Jurg Schrank	Pharmaceutical preparations
FR2521565B1 (fr)	1982-02-17	1985-07-05	Dior Sa Parfums Christian	Melange pulverulent de constituants lipidiques et de constituants hydrophobes, procede pour le preparer, phases lamellaires lipidiques hydratees et procede de fabrication, compositions pharmaceutiques ou cosmetiques comportant des phases lamellaires lipidiques hydratees
US4880635B1 (en)	1984-08-08	1996-07-02	Liposome Company	Dehydrated liposomes
US4857319A (en)	1985-01-11	1989-08-15	The Regents Of The University Of California	Method for preserving liposomes
US5178875A (en) *	1991-01-14	1993-01-12	The Board Of Regents, The University Of Texas System	Liposomal-polyene preliposomal powder and method for its preparation
CA1335077C (en) *	1988-02-08	1995-04-04	Henri Isliker	Process for the manufacture of apolipoproteins from human blood plasma or serum
US5077057A (en) *	1989-04-05	1991-12-31	The Regents Of The University Of California	Preparation of liposome and lipid complex compositions
US5753258A (en) *	1990-10-19	1998-05-19	University Of Florida	Artificial viral envelopes
DE69321118T2 (de) *	1992-06-12	1999-06-02	Innogenetics Nv	Peptide und Proteine, Verfahren zur Ihren Herstellung und die Verwendung als Cholesterol-Annehmer
US5785984A (en) *	1993-02-05	1998-07-28	Kao Corporation	Taste-modifying method and bitterness-decreasing method
US5534241A (en) *	1993-07-23	1996-07-09	Torchilin; Vladimir P.	Amphipathic polychelating compounds and methods of use
US5652339A (en) *	1993-12-31	1997-07-29	Rotkreuzstiftung Zentrallaboratorium	Method of producing reconstituted lipoproteins
DE4416166C2 (de) *	1994-05-06	1997-11-20	Immuno Ag	Stabiles Präparat zur Behandlung von Blutgerinnungsstörungen
US5948756A (en) *	1995-08-31	1999-09-07	Yissum Research Development Company Of The Hebrew University Of Jerusalem	Therapeutic lipoprotein compositions
US6004925A (en) *	1997-09-29	1999-12-21	J. L. Dasseux	Apolipoprotein A-I agonists and their use to treat dyslipidemic disorders
US6287590B1 (en)	1997-10-02	2001-09-11	Esperion Therapeutics, Inc.	Peptide/lipid complex formation by co-lyophilization

1997
- 1997-10-02 US US08/942,597 patent/US6287590B1/en not_active Expired - Fee Related
1998
- 1998-09-28 CN CNB988118181A patent/CN100415210C/zh not_active Expired - Fee Related
- 1998-09-28 NZ NZ503721A patent/NZ503721A/en not_active IP Right Cessation
- 1998-09-28 DE DE69822176T patent/DE69822176T2/de not_active Expired - Lifetime
- 1998-09-28 AT AT98950743T patent/ATE260644T1/de not_active IP Right Cessation
- 1998-09-28 UA UA2000042492A patent/UA71551C2/uk unknown
- 1998-09-28 AU AU96715/98A patent/AU749344B2/en not_active Ceased
- 1998-09-28 HU HU0003930A patent/HUP0003930A3/hu unknown
- 1998-09-28 JP JP2000514617A patent/JP2001522781A/ja not_active Withdrawn
- 1998-09-28 ES ES98950743T patent/ES2217591T3/es not_active Expired - Lifetime
- 1998-09-28 DK DK98950743T patent/DK1019025T3/da active
- 1998-09-28 RU RU2000111523/15A patent/RU2224506C2/ru not_active IP Right Cessation
- 1998-09-28 PT PT98950743T patent/PT1019025E/pt unknown
- 1998-09-28 KR KR1020007003586A patent/KR100588241B1/ko not_active IP Right Cessation
- 1998-09-28 EP EP98950743A patent/EP1019025B1/en not_active Expired - Lifetime
- 1998-09-28 WO PCT/US1998/020330 patent/WO1999017740A1/en active IP Right Grant
- 1998-09-28 EP EP03015963A patent/EP1358874A1/en not_active Withdrawn
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- 1998-09-28 CA CA002305704A patent/CA2305704C/en not_active Expired - Fee Related
- 1998-09-28 PL PL339654A patent/PL196579B1/pl not_active IP Right Cessation
2000
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- 2000-08-21 US US09/642,363 patent/US6455088B1/en not_active Expired - Fee Related
2002
- 2002-08-12 AU AU2002300504A patent/AU2002300504B2/en not_active Ceased
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Also Published As

Publication number	Publication date
US6287590B1 (en)	2001-09-11
KR100588241B1 (ko)	2006-06-13
CN100415210C (zh)	2008-09-03
US7189411B2 (en)	2007-03-13
RU2224506C2 (ru)	2004-02-27
NO329155B1 (no)	2010-08-30
PT1019025E (pt)	2004-07-30
NO20001683L (no)	2000-05-10
US20070167351A1 (en)	2007-07-19
AU2002300504B2 (en)	2005-05-12
EP1019025A4 (en)	2001-10-24
CA2305704A1 (en)	1999-04-15
EP1019025B1 (en)	2004-03-03
DE69822176D1 (de)	2004-04-08
CN1280490A (zh)	2001-01-17
HUP0003930A3 (en)	2001-06-28
US6455088B1 (en)	2002-09-24
HUP0003930A2 (hu)	2001-05-28
NO20001683D0 (no)	2000-03-31
AU9671598A (en)	1999-04-27
CA2305704C (en)	2008-09-30
PL196579B1 (pl)	2008-01-31
ES2217591T3 (es)	2004-11-01
DK1019025T3 (da)	2004-05-24
US20030099714A1 (en)	2003-05-29
ATE260644T1 (de)	2004-03-15
JP2001522781A (ja)	2001-11-20
NZ503721A (en)	2001-08-31
IL135322A0 (en)	2001-05-20
WO1999017740A1 (en)	1999-04-15
KR20010030892A (ko)	2001-04-16
EP1358874A1 (en)	2003-11-05
WO1999017740A9 (en)	1999-08-05
EP1019025A1 (en)	2000-07-19
DE69822176T2 (de)	2004-09-16
AU749344B2 (en)	2002-06-27
PL339654A1 (en)	2001-01-02
IL135322A (en)	2005-11-20

Publication	Publication Date	Title
UA71551C2 (en)	2004-12-15	Formation of peptide/lipid vesicles and complexes through co-lyophilization of peptides
FI86371C (fi)	1992-08-25	Foerfarande foer framstaellning av farmaceutiska liposomkompositioner.
FI63856B (fi)	1983-05-31	Foerfarande foer framstaellning av liposom-precursorer
EP0555229B1 (en)	1996-06-05	Accumulation of amino acids and peptides into liposomes
RU2000111523A (ru)	2002-05-10	Образование пептид/липидного комплекса путем совместной лиофилизации
WO2012109162A1 (en)	2012-08-16	Lipoprotein complexes and manufacturing and uses thereof
ES2236919T3 (es)	2005-07-16	Metodo para preparar composiciones farmaceuticas de particulas lipidicas que comprenden un agente lipidico y una proteina.
CA2221310A1 (en)	1996-12-19	Improved liposomal formulation
WO1991004019A1 (en)	1991-04-04	Therapeutic peptides and proteins
IE911231A1 (en)	1991-10-23	Long-acting liposome peptide pharmaceutical products and¹processes for the preparation thereof
Cserhåti et al.	1994	Interaction of phospholipids with proteins and peptides. New advances IV
JPS6362490B2 (no)	1988-12-02
MXPA00003132A (en)	2002-02-26	Peptide/lipid complex formation by co-lyophilization