Tetrapeptide derived inhibitors of complexation of a class II MHC: the peptide backbone is not inviolate

A B Jones; J J Acton 3rd; M N Rivetna; R T Cummings; R M Cubbon; E A Nichols; C D Schwartz; L S Wicker; J D Hermes

doi:10.1016/s0960-894x(99)00333-9

Tetrapeptide derived inhibitors of complexation of a class II MHC: the peptide backbone is not inviolate

Bioorg Med Chem Lett. 1999 Jul 19;9(14):2109-14. doi: 10.1016/s0960-894x(99)00333-9.

Authors

A B Jones¹, J J Acton 3rd, M N Rivetna, R T Cummings, R M Cubbon, E A Nichols, C D Schwartz, L S Wicker, J D Hermes

Affiliation

¹ Department of Basic Medicinal Chemistry, Merck Research Laboratories, Rahway, NJ 07065, USA.

PMID: 10450991
DOI: 10.1016/s0960-894x(99)00333-9

Abstract

Major histocompatabilty (MHC) proteins rely heavily on peptide backbone recognition for ligation. Nonetheless, modifications to the polyamide backbone of a tetrapeptide ligand can be made without abrogating binding.

MeSH terms

Binding Sites
HLA-DR1 Antigen / drug effects
HLA-DR1 Antigen / metabolism
Hemagglutinins / chemistry
Histocompatibility Antigens Class II / drug effects*
Histocompatibility Antigens Class II / metabolism*
Inhibitory Concentration 50
Lactams / chemistry
Ligands
Molecular Mimicry
Molecular Structure
Peptides / chemistry*
Peptides / pharmacology*
Phosphoproteins / drug effects
Phosphoproteins / metabolism
Structure-Activity Relationship
Transcription Factors / drug effects
Transcription Factors / metabolism

Substances

HLA-DR1 Antigen
Hemagglutinins
Histocompatibility Antigens Class II
Lactams
Ligands
Peptides
Phosphoproteins
Transcription Factors
down-regulator of transcription 1