α-Helix mimetics: Outwards and upwards

被引：92

作者：

Jayatunga, Madura K. P. ^{[1
]}

Thompson, Sam ^{[1
]}

Hamilton, Andrew D. ^{[1
]}

机构：

[1] Univ Oxford, Dept Chem, Chem Res Lab, Oxford OX1 3TA, England

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2014年 / 24卷 / 03期

关键词：

Protein-protein interaction; Rational design; Peptidomimetic; Proteomimetic; PROTEIN SURFACE RECOGNITION; SMALL-MOLECULE INHIBITORS; SOLID-PHASE SYNTHESIS; HYDROGEN-BOND; BETA-PEPTIDES; STRUCTURAL-CHARACTERIZATION; SECONDARY STRUCTURE; DESIGN; ACID; BINDING;

D O I：

10.1016/j.bmcl.2013.12.003

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

alpha-Helices are common secondary structural elements forming key parts of the large, generally featureless interfacial regions of many therapeutically-relevant protein-protein interactions (PPIs). The rational design of helix mimetics is an appealing small-molecule strategy for the mediation of aberrant PPIs, however the first generation of scaffolds presented a relatively small number of residues on a single recognition surface. Increasingly, helices involved in PPIs are found to have more complex binding modes, utilizing two or three recognition surfaces, or binding with extended points of contact. To address these unmet needs the design and synthesis of new generations of multi-sided, extended, and supersecondary structures are underway. (C) 2013 The Authors. Published by Elsevier Ltd. All rights reserved.

引用

页码：717 / 724

页数：8

共 114 条

[1] The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2 [J].

Abbate, EA ;

Berger, JM ;

Botchan, MR .

GENES & DEVELOPMENT, 2004, 18 (16) :1981-1996

[2] Oligophenylenaminones as Scaffolds for α-Helix Mimicry [J].

Adler, Marc J. ;

Hamilton, Andrew D. .

JOURNAL OF ORGANIC CHEMISTRY, 2011, 76 (17) :7040-7047

[3]

Ahn J. M., 2013, U.S. Patent, Patent No. [066,212, 066212]

[4]

Ahn J. M., 2008, U.S. Patent, Patent No. [056,920, 056920]

[5]

[Anonymous], MMFF94S CHEM COMP GR

[6] Synthesis and structural characterization of helix-forming β-peptides:: trans-2-aminocyclopentanecarboxylic acid oligomers [J].

Appella, DH ;

Christianson, LA ;

Klein, DA ;

Richards, MR ;

Powell, DR ;

Gellman, SH .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (33) :7574-7581

[7] Residue-based control of helix shape in beta-peptide oligomers [J].

Appella, DH ;

Christianson, LA ;

Klein, DA ;

Powell, DR ;

Huang, XL ;

Barchi, JJ ;

Gellman, SH .

NATURE, 1997, 387 (6631) :381-384

[8] Formation of short, stable helices in aqueous solution by β-amino acid hexamers [J].

Appella, DH ;

Barchi, JJ ;

Durell, SR ;

Gellman, SH .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (10) :2309-2310

[9] beta-peptide foldamers: Robust Helix formation in a new family of beta-amino acid oligomers [J].

Appella, DH ;

Christianson, LA ;

Karle, IL ;

Powell, DR ;

Gellman, SH .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (51) :13071-13072

[10] Computation-Guided Backbone Grafting of a Discontinuous Motif onto a Protein Scaffold [J].

Azoitei, Mihai L. ;

Correia, Bruno E. ;

Ban, Yih-En Andrew ;

Carrico, Chris ;

Kalyuzhniy, Oleksandr ;

Chen, Lei ;

Schroeter, Alexandria ;

Huang, Po-Ssu ;

McLellan, Jason S. ;

Kwong, Peter D. ;

Baker, David ;

Strong, Roland K. ;

Schief, William R. .

SCIENCE, 2011, 334 (6054) :373-376

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