Rational design of alpha-helical antifreeze peptides.
The alanine-rich alpha-helical antifreeze protein from the winter flounder Pseudopleuronectes americanus adsorbs to specific planes of ice guided by an ice lattice match to threonine residues regularly spaced 16.6 A apart. We report here that by redesigning the winter flounder antifreeze peptide to incorporate a 27.1-A spacing between putative 'ice-binding' threonines, the deduced binding alignment of the helical molecule on the ice lattice is changed from the Miller indices directional vector [1102 ] to [2203 ]. Subsequent ice-binding characteristics are altered, including changes in adsorption specificity, decreases in thermal hysteresis activity and the formation of rotated hexagonal bipyramid ice crystal morphology.
Kuiper
M J
MJ
School of Engineering and Science, Swinburne University of Technology, Hawthorn, Victoria, Australia.
Fecondo
J V
JV
Wong
M G
MG
D000595:Amino Acid Sequence; D021301:Antifreeze Proteins / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D003460:Crystallization; D015195:Drug Design; D007053:Ice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary
D021301:Antifreeze Proteins; D007053:Ice