TY - JOUR
T1 - Aggregation properties of mycolic acid molecules in monolayer films
T2 - A comparative study of compounds from various acid-fast bacterial species
AU - Hasegawa, Takeshi
AU - Leblanc, Roger M.
N1 - Funding Information:
The authors greatly thank Dr. Motoko Watanabe for very kindly providing us with the high-quality MAs extracted from the living bacterial masses. This work was financially aided by Grant-in-Aid for Scientific Research on Priority Areas (A), “Dynamic Control of Strongly Correlated Soft Materials” (no. 413/14045267) from the Ministry of Education, Science, Sports, Culture, and Technology.
PY - 2003/10/31
Y1 - 2003/10/31
N2 - Three kinds of mycolic acids (MAs) (α-, keto and methoxy-MAs) extracted from several species of mycobacteria were used to prepare monolayer films on water, and the surface pressure-area (π-A) isotherms of the monolayers have been compared, so that the monolayer characteristics of the MAs as in cell walls would be revealed, since the monolayer molecular aggregation is related to drug permeability via the molecular packing. It was expected that the limiting molecular areas of the isotherms would be changed only a little, which reflects the minor difference in chemical structure and conformation of the mycobacteria. Nevertheless, the results are largely different from the expectation, and two greatly different patterns of the limiting molecular area have been observed. In a new model for elucidation of the results, two parts in an MA molecule are separately considered, and both contributions to the molecular unfolding by the monolayer compression have been suggested. This model is found to be useful to totally understand the isotherm behaviors of MAs. The relationship between monolayer properties and chemical structures for MAs has been summarized for the first time.
AB - Three kinds of mycolic acids (MAs) (α-, keto and methoxy-MAs) extracted from several species of mycobacteria were used to prepare monolayer films on water, and the surface pressure-area (π-A) isotherms of the monolayers have been compared, so that the monolayer characteristics of the MAs as in cell walls would be revealed, since the monolayer molecular aggregation is related to drug permeability via the molecular packing. It was expected that the limiting molecular areas of the isotherms would be changed only a little, which reflects the minor difference in chemical structure and conformation of the mycobacteria. Nevertheless, the results are largely different from the expectation, and two greatly different patterns of the limiting molecular area have been observed. In a new model for elucidation of the results, two parts in an MA molecule are separately considered, and both contributions to the molecular unfolding by the monolayer compression have been suggested. This model is found to be useful to totally understand the isotherm behaviors of MAs. The relationship between monolayer properties and chemical structures for MAs has been summarized for the first time.
KW - Chain folding
KW - Molecular aggregation property
KW - Molecular conformation
KW - Mycolic acid
UR - http://www.scopus.com/inward/record.url?scp=0344154519&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0344154519&partnerID=8YFLogxK
U2 - 10.1016/j.bbamem.2003.09.008
DO - 10.1016/j.bbamem.2003.09.008
M3 - Article
C2 - 14637023
AN - SCOPUS:0344154519
VL - 1617
SP - 89
EP - 95
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
SN - 0005-2736
IS - 1-2
ER -