TY - JOUR
T1 - Antifreeze glycoprotein agents
T2 - Structural requirements for activity
AU - Carvajal-Rondanelli, Patricio A.
AU - Marshall, Sergio H.
AU - Guzman, Fanny
PY - 2011/11
Y1 - 2011/11
N2 - Antifreeze glycoproteins (AFGPs) are considered to be the most efficient means to reduce ice damage to cell tissues since they are able to inhibit growth and crystallization of ice. The key element of antifreeze proteins is to act in a non-colligative manner which allows them to function at concentrations 300-500 times lowers than other dissolved solutes. During the past decade, AFGPs have demonstrated tremendous potential for many pharmaceutical and food applications. Presently, the only route to obtain AFGPs involves the time consuming and expensive process of isolation and purification from deep-sea polar fishes. Unfortunately, it is not amenable to mass production and commercial applications. The lack of understanding of the mechanism through which the AFGPs inhibit ice growth has also hampered the realization of industrial and biotechnological applications. Here we report the structural motifs that are essential for antifreeze activity of AFGPs, and propose a unified mechanism based on both recent studies of short alanine peptides and structure activity relationship of synthesized AFGPs.
AB - Antifreeze glycoproteins (AFGPs) are considered to be the most efficient means to reduce ice damage to cell tissues since they are able to inhibit growth and crystallization of ice. The key element of antifreeze proteins is to act in a non-colligative manner which allows them to function at concentrations 300-500 times lowers than other dissolved solutes. During the past decade, AFGPs have demonstrated tremendous potential for many pharmaceutical and food applications. Presently, the only route to obtain AFGPs involves the time consuming and expensive process of isolation and purification from deep-sea polar fishes. Unfortunately, it is not amenable to mass production and commercial applications. The lack of understanding of the mechanism through which the AFGPs inhibit ice growth has also hampered the realization of industrial and biotechnological applications. Here we report the structural motifs that are essential for antifreeze activity of AFGPs, and propose a unified mechanism based on both recent studies of short alanine peptides and structure activity relationship of synthesized AFGPs.
KW - AFGP
KW - Antifreeze glycoprotein
KW - Ice crystal inhibition
KW - Poly-L-proline II
KW - Protein hydration
UR - http://www.scopus.com/inward/record.url?scp=80053908961&partnerID=8YFLogxK
U2 - 10.1002/jsfa.4473
DO - 10.1002/jsfa.4473
M3 - Short survey
C2 - 21725975
AN - SCOPUS:80053908961
VL - 91
SP - 2507
EP - 2510
JO - Journal of the Science of Food and Agriculture
JF - Journal of the Science of Food and Agriculture
SN - 0022-5142
IS - 14
ER -