A biodegradable multiblock co-polymer derived from an alpha,omega-bis(methylamino)peptide and an alpha,omega-bis(oxiranylmethyl)poly(ethylene glycol)

Susan E. Matthews; Colin W. Pouton; Michael D. Threadgill

doi:10.1016/S0168-3659(00)00203-0

A biodegradable multiblock co-polymer derived from an alpha,omega-bis(methylamino)peptide and an alpha,omega-bis(oxiranylmethyl)poly(ethylene glycol)

Susan E. Matthews, Colin W. Pouton, Michael D. Threadgill

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

Abstract

A novel peptide containing the lysosomally degradable sequence GlyPheLeuGly and a sequence-inverting unit has been prepared. This peptide presents the methylamino groups of sarcosine (N-methylglycine) at both termini for co-polymerisation with alpha,omega-bis(oxiranylmethoxy)poly(ethylene glycol) of mean M-w 1650. Gel permeation chromatographic analysis showed the presence of a mixture of oligomers. preliminary degradation studies showed that these oligomers are cleaved by cathepsin B, an important lysosomal enzyme. (C) 2000 Elsevier Science B.V. All rights reserved.

Original language	English
Pages (from-to)	129-139
Number of pages	11
Journal	Journal of Controlled Release
Volume	67
Issue number	2-3
DOIs	https://doi.org/10.1016/S0168-3659(00)00203-0
Publication status	Published - 2000

Keywords

ETHERS
biodegradable
peptide
GlyPheLeuGly
PRODRUGS
COPOLYMERS
DRUG
DERIVATIVES
cathepsin B
polyethylene glycol
ENZYMATICALLY DEGRADABLE BONDS
RELEASE
retro-inverso
CARRIERS

Access to Document

10.1016/S0168-3659(00)00203-0

Cite this

@article{d65c49a72a384e888e5fa20444fe9091,

title = "A biodegradable multiblock co-polymer derived from an alpha,omega-bis(methylamino)peptide and an alpha,omega-bis(oxiranylmethyl)poly(ethylene glycol)",

abstract = "A novel peptide containing the lysosomally degradable sequence GlyPheLeuGly and a sequence-inverting unit has been prepared. This peptide presents the methylamino groups of sarcosine (N-methylglycine) at both termini for co-polymerisation with alpha,omega-bis(oxiranylmethoxy)poly(ethylene glycol) of mean M-w 1650. Gel permeation chromatographic analysis showed the presence of a mixture of oligomers. preliminary degradation studies showed that these oligomers are cleaved by cathepsin B, an important lysosomal enzyme. (C) 2000 Elsevier Science B.V. All rights reserved.",

keywords = "ETHERS, biodegradable, peptide, GlyPheLeuGly, PRODRUGS, COPOLYMERS, DRUG, DERIVATIVES, cathepsin B, polyethylene glycol, ENZYMATICALLY DEGRADABLE BONDS, RELEASE, retro-inverso, CARRIERS",

author = "Matthews, {Susan E.} and Pouton, {Colin W.} and Threadgill, {Michael D.}",

year = "2000",

doi = "10.1016/S0168-3659(00)00203-0",

language = "English",

volume = "67",

pages = "129--139",

journal = "Journal of Controlled Release",

issn = "0168-3659",

publisher = "Elsevier",

number = "2-3",

}

TY - JOUR

T1 - A biodegradable multiblock co-polymer derived from an alpha,omega-bis(methylamino)peptide and an alpha,omega-bis(oxiranylmethyl)poly(ethylene glycol)

AU - Matthews, Susan E.

AU - Pouton, Colin W.

AU - Threadgill, Michael D.

PY - 2000

Y1 - 2000

N2 - A novel peptide containing the lysosomally degradable sequence GlyPheLeuGly and a sequence-inverting unit has been prepared. This peptide presents the methylamino groups of sarcosine (N-methylglycine) at both termini for co-polymerisation with alpha,omega-bis(oxiranylmethoxy)poly(ethylene glycol) of mean M-w 1650. Gel permeation chromatographic analysis showed the presence of a mixture of oligomers. preliminary degradation studies showed that these oligomers are cleaved by cathepsin B, an important lysosomal enzyme. (C) 2000 Elsevier Science B.V. All rights reserved.

AB - A novel peptide containing the lysosomally degradable sequence GlyPheLeuGly and a sequence-inverting unit has been prepared. This peptide presents the methylamino groups of sarcosine (N-methylglycine) at both termini for co-polymerisation with alpha,omega-bis(oxiranylmethoxy)poly(ethylene glycol) of mean M-w 1650. Gel permeation chromatographic analysis showed the presence of a mixture of oligomers. preliminary degradation studies showed that these oligomers are cleaved by cathepsin B, an important lysosomal enzyme. (C) 2000 Elsevier Science B.V. All rights reserved.

KW - ETHERS

KW - biodegradable

KW - peptide

KW - GlyPheLeuGly

KW - PRODRUGS

KW - COPOLYMERS

KW - DRUG

KW - DERIVATIVES

KW - cathepsin B

KW - polyethylene glycol

KW - ENZYMATICALLY DEGRADABLE BONDS

KW - RELEASE

KW - retro-inverso

KW - CARRIERS

U2 - 10.1016/S0168-3659(00)00203-0

DO - 10.1016/S0168-3659(00)00203-0

M3 - Article

SN - 0168-3659

VL - 67

SP - 129

EP - 139

JO - Journal of Controlled Release

JF - Journal of Controlled Release

IS - 2-3

ER -