Effect of amino acid distribution of amphipathic helical peptide derived from human apolipoprotein A-I on membrane curvature sensing

FEBS Letters ◽  
2013 ◽  
Vol 587 (5) ◽  
pp. 510-515 ◽  
Author(s):  
Masafumi Tanaka ◽  
Yuki Takamura ◽  
Toru Kawakami ◽  
Saburo Aimoto ◽  
Hiroyuki Saito ◽  
...  
Keyword(s):  
Amino Acid ◽  
Membrane Curvature ◽  
Amino Acid Distribution ◽  
Curvature Sensing ◽  
Human Apolipoprotein ◽  
Apolipoprotein A ◽  
Helical Peptide

scholarly journals Amphipathic helical peptide-based fluorogenic probes for a marker-free analysis of exosomes based on membrane-curvature sensing

RSC Advances ◽  
2020 ◽  
Vol 10 (63) ◽  
pp. 38323-38327
Author(s):  
Yusuke Sato ◽  
Kazuki Kuwahara ◽  
Kenta Mogami ◽  
Kenta Takahashi ◽  
Seiichi Nishizawa
Keyword(s):  
Membrane Curvature ◽  
Helical Peptides ◽  
Curvature Sensing ◽  
Helical Peptide ◽  
Fluorogenic Probes ◽  
Marker Free

Fluorogenic probes based on membrane curvature sensing-amphipathic helical peptides have been developed for a marker-free exosome analysis.

scholarly journals Deletion of Single Amino Acid E235 Affects the Structure and Lipid Interaction of Human Apolipoprotein A-I C-Terminal Peptides

2009 ◽  
Vol 57 (5) ◽  
pp. 499-503 ◽  
Author(s):  
Toshitaka Tanaka ◽  
Masafumi Tanaka ◽  
Makiko Sugiura ◽  
Toru Kawakami ◽  
Saburo Aimoto ◽  
...  
Keyword(s):  
Amino Acid ◽  
Single Amino Acid ◽  
Human Apolipoprotein ◽  
Apolipoprotein A ◽  
Lipid Interaction

scholarly journals PHYLOGENIES CONSTRAINED BY THE CROSSOVER PROCESS AS ILLUSTRATED BY HUMAN HEMOGLOBINS AND A THIRTEEN-CYCLE, ELEVEN-AMINO-ACID REPEAT IN HUMAN APOLIPOPROTEIN A-I

Genetics ◽  
1977 ◽  
Vol 86 (3) ◽  
pp. 623-644
Author(s):  
Walter M Fitch
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Chemical Properties ◽  
Blood Stream ◽  
Crossing Over ◽  
Alpha Helices ◽  
Unequal Crossing Over ◽  
Human Apolipoprotein ◽  
Apolipoprotein A ◽  
The Right

ABSTRACT Examination of human apolipoprotein A-I revealed a segment of eleven amino acids that repeated itself 13 times in succession without any additional intervening amino acids between the beginning of the repeats (amino acid 93) and their end at the carboxyl terminus of the sequence. The segments are not identical, but the pattern of their physical and chemical properties is highly conserved. The pattern is shown to be suitable to the formation of alpha helices with an amphipathic character consistent with the formation of a micellar structure, a process entirely appropriate to the protein's known function in the blood stream as a lipid carrier. The simplest hypothesis to account for repeated segments is a series of unequal crossovers. But such a series implies that some segments are more closely related to each other than they are to others, that is, they have a "phylogenetic" relationship. It is shown that only a small fraction of all possible phylogenies are consistent with a set of segments arising by simple unequal crossing over. Nevertheless, it is shown that the apolipoprotein A-I segments are readily interpretable as the result of simple unequal crossing over. Moreover, the crossover constraint applies with as much force to segments larger than a gene as to segments within a gene, and this is shown to require that the human gamma (Gly) hemoglobin gene lie to the left, rather than to the right, of the other non-alpha human hemoglobin genes, a conclusion for which there is no direct genetic evidence currently available.

Inhibition of Atherosclerosis Development in Cholesterol-Fed Human Apolipoprotein A-I–Transgenic Rabbits

Circulation ◽  
1996 ◽  
Vol 94 (4) ◽  
pp. 713-717 ◽  
Author(s):  
Nicolas Duverger ◽  
Howard Kruth ◽  
Florence Emmanuel ◽  
Jean-Michel Caillaud ◽  
Ce´line Viglietta ◽  
...  
Keyword(s):  
Human Apolipoprotein ◽  
Apolipoprotein A ◽  
Transgenic Rabbits ◽  
Atherosclerosis Development
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