TY - JOUR
T1 - Synthesis and evaluation of linear CuAAC-oligomerized antifreeze neo-glycopeptides
AU - Van Der Wal, Steffen
AU - Capicciotti, Chantelle J.
AU - Rontogianni, Stamatia
AU - Ben, Robert N.
AU - Liskamp, Rob M J
PY - 2014
Y1 - 2014
N2 - Antifreeze glycoproteins (AFGPs) are important naturally occurring biological antifreezes that lower the freezing point of a solution, thereby preventing uncontrolled ice growth. These compounds also inhibit ice recrystallization. Described in this paper is a synthetic antifreeze glycopeptide-based polymer synthesized from an azide/alkyne glycopeptide building block by partial reduction of the azide and subsequent copper catalyzed azide alkyne cycloaddition (CuAAC) polymerization to obtain linear oligomers. To compare the activity with native AFGPs, a linear dodecapeptide (oligomer with four repeating units) was synthesized and isolated which had a comparable length to AFGP-8, the lowest molecular mass glycoprotein AFGP found in nature. In terms of ice recrystallization inhibition (IRI) activity, the triazole-based oligomers displayed only modest IRI activity compared with AFGP-8 and a previously described carbon-linked AFGP analogue. However, CD spectroscopy showed that the triazole-based tetramer possessed a similar secondary structure to the related amide based carbon-linked AFGP tetramer based on AFGP-8. This journal is
AB - Antifreeze glycoproteins (AFGPs) are important naturally occurring biological antifreezes that lower the freezing point of a solution, thereby preventing uncontrolled ice growth. These compounds also inhibit ice recrystallization. Described in this paper is a synthetic antifreeze glycopeptide-based polymer synthesized from an azide/alkyne glycopeptide building block by partial reduction of the azide and subsequent copper catalyzed azide alkyne cycloaddition (CuAAC) polymerization to obtain linear oligomers. To compare the activity with native AFGPs, a linear dodecapeptide (oligomer with four repeating units) was synthesized and isolated which had a comparable length to AFGP-8, the lowest molecular mass glycoprotein AFGP found in nature. In terms of ice recrystallization inhibition (IRI) activity, the triazole-based oligomers displayed only modest IRI activity compared with AFGP-8 and a previously described carbon-linked AFGP analogue. However, CD spectroscopy showed that the triazole-based tetramer possessed a similar secondary structure to the related amide based carbon-linked AFGP tetramer based on AFGP-8. This journal is
UR - http://www.scopus.com/inward/record.url?scp=84904804902&partnerID=8YFLogxK
U2 - 10.1039/c4md00013g
DO - 10.1039/c4md00013g
M3 - Article
AN - SCOPUS:84904804902
SN - 2040-2503
VL - 5
SP - 1159
EP - 1165
JO - MedChemComm
JF - MedChemComm
IS - 8
ER -