当前位置： SCI文献检索 > BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS期刊下所有文献 > Affinity selection to papain yields potent peptide inhibitors of cathepsins L, B, H, and K.

Affinity selection to papain yields potent peptide inhibitors of cathepsins L, B, H, and K.

Abstract：

:Endogenous cysteine proteases were given much attention lately, as their role in a variety of pathophysiological disorders became evident. Amongst them cathepsins, which are thought to be implicated in mediation of osteoporosis, cancer progression, atherosclerosis, and many other conditions, are of considerable interest as drug targets. In the presented work, papain was chosen as a model cysteine protease and panning protocol was optimized for selection of papain-binding phage-displayed peptides from a commercially available combinatorial peptide library. Different selection strategies were applied in order to select high-affinity binders. Ultimately, five cyclic peptides (CNWAAGYNCGGGS-NH2, CWSMMGFQCGGGS-NH2, CWEWGGWHCGGSS-OH, CNWTLGGYKCGGGS-NH2 (all cyclized through formation of intramolecular disulphide bond), and GNWTLGGYKGG (cyclized head-to-tail)) were synthesized and tested for inhibitory activity towards papain and human cathepsins L, B, H, and K. The peptides possess inhibitory constants in the low micromolar to mid-nanomolar range and exhibit certain selectivity for different lysosomal cysteine proteases included in this study.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Bratkovic T,Lunder M,Popovic T,Kreft S,Turk B,Strukelj B,Urleb U

doi

10.1016/j.bbrc.2005.05.028

subject

Has Abstract

pub_date

2005-07-08 00:00:00

pages

897-903

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)01001-6

journal_volume

332

pub_type

杂志文章

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