Libraries soluble peptide

Glycosylation of peptides is an efficient method to stabilize peptide by inhibition of enzymatic degradation, to conformationally modify peptide and usually to increase peptide solubility. Peptides glycosylation also creates additional diversity in peptide libraries since the high functionalities and variability of sugar moieties. 

Pinilla C, Appel J, Blondelle S, Dooley C, Domer B, Eichler J, Ostresh J, Houghten RA, A review of the utility of soluble peptide combinatorial libraries, Biopolymers, 37(3) 221-240, 1995. 

Reported applications of the technique to combinatorial syntheses include libraries of peptides ([69,71,72]), 4-amino-benzenesulfonamides ([69,71,72]), and peptidomimetics (poly-a-aza-amino acids or azatides, [69,71,73]). The latter synthesis also illustrates one of the advantages of the soluble polymer approach over solid-phase synthesis, namely. 

Huang, P.Y. and Carbonell, R.G., Affinity chromatographic screening of soluble combinatorial peptide libraries, Biotechnol. Bioeng., 63, 633-641, 2000. 

A demonstration of liquid-phase combinatorial synthesis was recently introduced whereby the highly soluble, but highly crystalline, monomethyl polyethylene glycol (PEG) was employed to allow solution synthesis of a peptide library and solid phase-like purification by a change to a solvent where the PEG was insoluble. The demonstration penta-peptide library yielded the expected anti-P-endorphin binding sequence [65]... 

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