915104-06-2Relevant academic research and scientific papers
Synthesis and structural investigations of N-alkylated β-peptidosulfonamide-peptide hybrids of the amyloidogenic amylin(20-29) sequence: Implications of supramolecular folding for the design of peptide-based bionanomaterials
Elgersma, Ronald C.,Meijneke, Tania,De Jong, Remco,Brouwer, Arwin J.,Posthuma, George,Rijkers, Dirk T. S.,Liskamp, Rob M. J.
, p. 3587 - 3597 (2008/10/09)
The incorporation of a single β-aminoethane sulfonyl amide moiety in a highly amyloidogenic peptide sequence resulted in a complete loss of amyloid fibril formation. Instead, supramolecular folding morphologies were observed. Subsequent chemoselective N-alkylation of the sulfonamide resulted in amphiphilic peptide-based hydrogelators. It was found that variation of merely the alkyl chain induced a dramatic variation in aggregation motifs such as helical ribbons and tapes, ribbons progressing to closed tubes, twisted lamellar sheets and entangled/branched fibers. The Royal Society of Chemistry 2006.
