Synthesis and structural investigations of N-alkylated beta-peptidosulfonamide-peptide hybrids of the amyloidogenic amylin(20-29) sequence: Implications of supramolecular folding for the design of peptide-based bionanomaterials.
The incorporation of a single beta-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.
Elgersma
Ronald C
RC
Department of Medicinal Chemistry and Chemical Biology, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, PO Box 80082, 3508 TB, Utrecht, The Netherlands.
Meijneke
Tania
T
de Jong
Remco
R
Brouwer
Arwin J
AJ
Posthuma
George
G
Rijkers
Dirk T S
DT
Liskamp
Rob M J
RM
D000595:Amino Acid Sequence; D000682:Amyloid / Q000138:chemical synthesis* / Q000737:chemistry* / Q000648:ultrastructure; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D005782:Gels; D058228:Islet Amyloid Polypeptide; D008969:Molecular Sequence Data; D049329:Nanostructures / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013449:Sulfonamides / Q000138:chemical synthesis* / Q000737:chemistry*
D000682:Amyloid; D005782:Gels; D058228:Islet Amyloid Polypeptide; D010455:Peptides; D013449:Sulfonamides