Fluoro-olefin Isosteres as Peptidomimetics

J. T. Welch; J. Lin; L. G. Boros; B. DeCorte; K. Bergmann; R. Gimi

doi:10.1021/bk-1996-0639.ch010

Fluoro-olefin Isosteres as Peptidomimetics

J. T. Welch
, J. Lin
, L. G. Boros
, B. DeCorte
, K. Bergmann
, R. Gimi

Chemistry

University at Albany

SUNY Albany
Albany Molecular Research
Johnson & Johnson
SRC, Inc.
Brookhaven National Laboratory

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

27 Scopus citations

Abstract

Fluroolefin dipeptide isosteres were synthesized applying the Peterson reaction as a novel method for fluoroolefination. Gly-ψ[CF=C]-Pro dipeptide isosteres were elaborated to provide conformationally constrained analogs of the Suc-Ala-Gly-Pro-Phe-pNA tetrapeptide substrate for cyclophilin. Ala-ψ[CF=C]-Pro containing N,O-diacylhydroxamic acid type protease inhibitors were synthesized for the study of the influence of prolylamide bond geometry on the inhibition of dipeptidyl peptidase IV(CD26).

Original language	English
Pages (from-to)	129-142
Number of pages	14
Journal	ACS Symposium Series
Volume	639
DOIs	https://doi.org/10.1021/bk-1996-0639.ch010
State	Published - 1996

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title = "Fluoro-olefin Isosteres as Peptidomimetics",

abstract = "Fluroolefin dipeptide isosteres were synthesized applying the Peterson reaction as a novel method for fluoroolefination. Gly-ψ[CF=C]-Pro dipeptide isosteres were elaborated to provide conformationally constrained analogs of the Suc-Ala-Gly-Pro-Phe-pNA tetrapeptide substrate for cyclophilin. Ala-ψ[CF=C]-Pro containing N,O-diacylhydroxamic acid type protease inhibitors were synthesized for the study of the influence of prolylamide bond geometry on the inhibition of dipeptidyl peptidase IV(CD26).",

author = "Welch, \{J. T.\} and J. Lin and Boros, \{L. G.\} and B. DeCorte and K. Bergmann and R. Gimi",

year = "1996",

doi = "10.1021/bk-1996-0639.ch010",

language = "English",

volume = "639",

pages = "129--142",

journal = "ACS Symposium Series",

issn = "0097-6156",

publisher = "American Chemical Society",

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T1 - Fluoro-olefin Isosteres as Peptidomimetics

AU - Welch, J. T.

AU - Lin, J.

AU - Boros, L. G.

AU - DeCorte, B.

AU - Bergmann, K.

AU - Gimi, R.

PY - 1996

Y1 - 1996

N2 - Fluroolefin dipeptide isosteres were synthesized applying the Peterson reaction as a novel method for fluoroolefination. Gly-ψ[CF=C]-Pro dipeptide isosteres were elaborated to provide conformationally constrained analogs of the Suc-Ala-Gly-Pro-Phe-pNA tetrapeptide substrate for cyclophilin. Ala-ψ[CF=C]-Pro containing N,O-diacylhydroxamic acid type protease inhibitors were synthesized for the study of the influence of prolylamide bond geometry on the inhibition of dipeptidyl peptidase IV(CD26).

AB - Fluroolefin dipeptide isosteres were synthesized applying the Peterson reaction as a novel method for fluoroolefination. Gly-ψ[CF=C]-Pro dipeptide isosteres were elaborated to provide conformationally constrained analogs of the Suc-Ala-Gly-Pro-Phe-pNA tetrapeptide substrate for cyclophilin. Ala-ψ[CF=C]-Pro containing N,O-diacylhydroxamic acid type protease inhibitors were synthesized for the study of the influence of prolylamide bond geometry on the inhibition of dipeptidyl peptidase IV(CD26).

UR - https://www.scopus.com/pages/publications/1842578410

U2 - 10.1021/bk-1996-0639.ch010

DO - 10.1021/bk-1996-0639.ch010

M3 - Article

SN - 0097-6156

VL - 639

SP - 129

EP - 142

JO - ACS Symposium Series

JF - ACS Symposium Series

ER -

Fluoro-olefin Isosteres as Peptidomimetics

Abstract

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