title: 4-ketoproline: An electrophilic proline analog for bioconjugation.
abstract: Installing an electrophilic amino-acid residue can engender a peptide or protein with chemoselective reactivity. Such a modification to collagen, which is the most abundant protein in animals, could facilitate the development of new biomaterials. Collagen has an abundance of proline-like residues. Here, we report on the incorporation of an electrophilic proline congener, (2S)-4-ketoproline (Kep), into a collagen-mimetic peptide (CMP). An ab initio conformational analysis of Kep revealed its potential to be accommodated within a collagen triple helix. A synthetic CMP containing a Kep residue was indeed able to form a stable triple helix. Moreover, the condensation of its carbonyl group with aminooxy-biotin did not compromise the conformational stability of the triple helix. These data encourage the use of 4-ketoproline as an electrophilic congener of proline.
authors: Graduate Program in Biophysics, University of Wisconsin-Madison, Madison, WI.
authors: Amit
authors: A
authors: Choudhary
authors: Kimberli J
authors: KJ
authors: Kamer
authors: Matthew D
authors: MD
authors: Shoulders
authors: Ronald T
authors: RT
authors: Raines
mesh_terms: D003094:Collagen / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D011392:Proline / Q000031:analogs & derivatives* / Q000737:chemistry; D011487:Protein Conformation
chemical_list: D010455:Peptides; C036784:4-ketoproline; D003094:Collagen; D011392:Proline
keywords: 4-ketoproline; 4-oxoproline; collagen; host-guest; oxime
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