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A flexible method for preparation of peptide homo‐ and heterodimers functionalized with affinity probes, chelating ligands, and latent conjugating groups
Author(s) -
Pillai Radhakrishna,
Marinelli Edmund R.,
Swenson Rolf E.
Publication year - 2006
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20570
Subject(s) - chemistry , bifunctional , linker , dimer , peptide , monomer , combinatorial chemistry , chelation , molecule , stereochemistry , lysine , preprint , binding affinities , amino acid , receptor , biochemistry , organic chemistry , polymer , world wide web , computer science , catalysis , operating system
Dimerization of peptides can provide high binding entities to serve as targeted diagnostics or therapeutics. We developed methods for the preparation of homo‐ and heterodimer peptides bearing functional molecules (affinity probes, chelating ligands, or latent conjugating moieties). Monomer peptides, optionally bearing spacer groups, are tethered using a bifunctional linker, (di‐succinimidyl glutarate, DSG) to provide the dimers. Protected or unprotected peptides can be employed for dimer assembly. Multiple lysine N ϵ ‐amino groups are controlled using the (4,4‐dimethyl‐2,6‐dioxocyclohex‐1‐ylidene)‐3‐methylbutyl (ivDde) protecting group. Functional molecules are optionally incorporated into the component peptides or into the assembled dimer. The methods are efficient and scaleable. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 576–585, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com