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URL: https://dx.doi.org/DOI:10.17504/protocols.io.bjibkkan

Authors: Angel Justiz-Vaillant

Summary: Chemical synthesis facilitates the generation of peptides which are exceedingly difficult to express in bacteria, peptide/protein backbone modification, the incorporation of unnatural amino acids, and the production or synthesis of D-proteins. The C-terminal cysteine can be added to the amino acidic sequences of HIV peptides (fragment 579-601 of the HIV-gp41 [1]. These peptide fragments were dimerized by cysteine oxidation with dimethyl-sulfoxide [2] to facilitate their conjugation to keyhole limpet hemocyanin that acts as a carrier protein. Reference:McPhee DA, Kemp BE, Cumming S, Stapleton D, Gust ID, Doherty RR. Recognition of envelope and tat protein synthetic peptide analogs by HIV positive sera or plasma. FEBS Lett. 1988;233(2):393-396. doi:10.1016/0014-5793(88)80468-x. Tam JP, Wu CR, Liu w, Zhang JW (1991) Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications. J Am Chem Soc 113: 66576662.

Affiliations: University of the West Indies St. Augustine

Version: 1

Publication Date: 2020

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