Rational Design of Constrained Peptides as Protein Interface Inhibitors

The lack of progress in developing targeted therapeutics directed at protein–protein complexes has been due to the absence of well-defined ligand-binding pockets and the extensive intermolecular contacts at the protein–protein interface. Our laboratory has developed approaches to dissect protein–pro...

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Main Authors:	Ramachandran Murali, Hongtao Zhang, Zheng Cai, Lian Lam, Mark Greene
Format:	Article
Language:	English
Published:	MDPI AG 2021-08-01
Series:	Antibodies
Subjects:	ErbB TNF mimetic receptor protein-engineering immunoadhesion
Online Access:	https://www.mdpi.com/2073-4468/10/3/32

id	doaj-491de3547c4b445795002bcab4ecdd3e
record_format	Article
spelling	doaj-491de3547c4b445795002bcab4ecdd3e2021-09-25T23:37:50ZengMDPI AGAntibodies2073-44682021-08-0110323210.3390/antib10030032Rational Design of Constrained Peptides as Protein Interface InhibitorsRamachandran Murali0Hongtao Zhang1Zheng Cai2Lian Lam3Mark Greene4Cedars-Sinai Medical Center, Department of Biomedical Science, Research Division of Immunology, Los Angeles, CA 90211, USADepartment of Pathology and Laboratory of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USADepartment of Pathology and Laboratory of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USADepartment of Pathology and Laboratory of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USADepartment of Pathology and Laboratory of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USAThe lack of progress in developing targeted therapeutics directed at protein–protein complexes has been due to the absence of well-defined ligand-binding pockets and the extensive intermolecular contacts at the protein–protein interface. Our laboratory has developed approaches to dissect protein–protein complexes focusing on the superfamilies of erbB and tumor necrosis factor (TNF) receptors by the combined use of structural biology and computational biology to facilitate small molecule development. We present a perspective on the development and application of peptide inhibitors as well as immunoadhesins to cell surface receptors performed in our laboratory.https://www.mdpi.com/2073-4468/10/3/32ErbBTNFmimeticreceptorprotein-engineeringimmunoadhesion
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Ramachandran Murali Hongtao Zhang Zheng Cai Lian Lam Mark Greene
spellingShingle	Ramachandran Murali Hongtao Zhang Zheng Cai Lian Lam Mark Greene Rational Design of Constrained Peptides as Protein Interface Inhibitors Antibodies ErbB TNF mimetic receptor protein-engineering immunoadhesion
author_facet	Ramachandran Murali Hongtao Zhang Zheng Cai Lian Lam Mark Greene
author_sort	Ramachandran Murali
title	Rational Design of Constrained Peptides as Protein Interface Inhibitors
title_short	Rational Design of Constrained Peptides as Protein Interface Inhibitors
title_full	Rational Design of Constrained Peptides as Protein Interface Inhibitors
title_fullStr	Rational Design of Constrained Peptides as Protein Interface Inhibitors
title_full_unstemmed	Rational Design of Constrained Peptides as Protein Interface Inhibitors
title_sort	rational design of constrained peptides as protein interface inhibitors
publisher	MDPI AG
series	Antibodies
issn	2073-4468
publishDate	2021-08-01
description	The lack of progress in developing targeted therapeutics directed at protein–protein complexes has been due to the absence of well-defined ligand-binding pockets and the extensive intermolecular contacts at the protein–protein interface. Our laboratory has developed approaches to dissect protein–protein complexes focusing on the superfamilies of erbB and tumor necrosis factor (TNF) receptors by the combined use of structural biology and computational biology to facilitate small molecule development. We present a perspective on the development and application of peptide inhibitors as well as immunoadhesins to cell surface receptors performed in our laboratory.
topic	ErbB TNF mimetic receptor protein-engineering immunoadhesion
url	https://www.mdpi.com/2073-4468/10/3/32
work_keys_str_mv	AT ramachandranmurali rationaldesignofconstrainedpeptidesasproteininterfaceinhibitors AT hongtaozhang rationaldesignofconstrainedpeptidesasproteininterfaceinhibitors AT zhengcai rationaldesignofconstrainedpeptidesasproteininterfaceinhibitors AT lianlam rationaldesignofconstrainedpeptidesasproteininterfaceinhibitors AT markgreene rationaldesignofconstrainedpeptidesasproteininterfaceinhibitors
_version_	1717368443258273792

Rational Design of Constrained Peptides as Protein Interface Inhibitors

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