TY - JOUR
T1 - Synthesis and characterization of natural and modified antifreeze glycopeptides
T2 - Glycosylated foldamers
AU - Nagel, Lilly
AU - Plattner, Carolin
AU - Budke, Carsten
AU - Majer, Zsuzsanna
AU - Devries, Arthur L.
AU - Berkemeier, Thomas
AU - Koop, Thomas
AU - Sewald, Norbert
N1 - Funding Information:
The authors gratefully acknowledge support from Deutsche Forschungsgemeinschaft (SFB 613, Project A8). L.N. was funded by a PhD fellowship of Bielefeld University.
PY - 2011/8
Y1 - 2011/8
N2 - In Arctic and Antarctic marine regions, where the temperature declines below the colligative freezing point of physiological fluids, efficient biological antifreeze agents are crucial for the survival of polar fish. One group of such agents is classified as antifreeze glycoproteins (AFGP) that usually consist of a varying number (n = 4-55) of [AAT] n -repeating units. The threonine side chain of each unit is glycosidically linked to β-d-galactosyl-(1 → 3)-α-N-acetyl-d-galactosamine. These biopolymers can be considered as biological antifreeze foldamers. A preparative route for stepwise synthesis of AFGP allows for efficient synthesis. The diglycosylated threonine building block was introduced into the peptide using microwave-enhanced solid phase synthesis. By this versatile solid phase approach, glycosylated peptides of varying sequences and lengths could be obtained. Conformational studies of the synthetic AFGP analogs were performed by circular dichroism experiments (CD). Furthermore, the foldamers were analysed microphysically according to their inhibiting effect on ice recrystallization and influence on the crystal habit.
AB - In Arctic and Antarctic marine regions, where the temperature declines below the colligative freezing point of physiological fluids, efficient biological antifreeze agents are crucial for the survival of polar fish. One group of such agents is classified as antifreeze glycoproteins (AFGP) that usually consist of a varying number (n = 4-55) of [AAT] n -repeating units. The threonine side chain of each unit is glycosidically linked to β-d-galactosyl-(1 → 3)-α-N-acetyl-d-galactosamine. These biopolymers can be considered as biological antifreeze foldamers. A preparative route for stepwise synthesis of AFGP allows for efficient synthesis. The diglycosylated threonine building block was introduced into the peptide using microwave-enhanced solid phase synthesis. By this versatile solid phase approach, glycosylated peptides of varying sequences and lengths could be obtained. Conformational studies of the synthetic AFGP analogs were performed by circular dichroism experiments (CD). Furthermore, the foldamers were analysed microphysically according to their inhibiting effect on ice recrystallization and influence on the crystal habit.
KW - Bioorganic chemistry
KW - Circular dichroism
KW - Glycopeptides
KW - Ice recrystallization
KW - Microwave-enhanced synthesis
KW - Solid phase peptide synthesis
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U2 - 10.1007/s00726-011-0937-8
DO - 10.1007/s00726-011-0937-8
M3 - Article
C2 - 21603949
AN - SCOPUS:80052325315
SN - 0939-4451
VL - 41
SP - 719
EP - 732
JO - Amino Acids
JF - Amino Acids
IS - 3
ER -