Effects of Fluidity on the Ensemble Structure of a Membrane Embedded α-Helical Peptide

被引:2
作者
Eagleburger, Michael K. [1 ]
Cooley, Jason W. [1 ]
Jiji, Renee D. [1 ]
机构
[1] Univ Missouri, Dept Chem, Columbia, MO 65211 USA
基金
美国国家科学基金会;
关键词
deep-UV resonance Raman spectroscopy; circular dichroism; melittin; membrane; UV RESONANCE RAMAN; PROTEIN SECONDARY STRUCTURE; CIRCULAR-DICHROISM SPECTRA; LIPID-COMPOSITION; MELITTIN; SPECTROSCOPY; MODEL; ANGLE; POLY(L-LYSINE); CONFORMATION;
D O I
10.1002/bip.22472
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Melittin, the main hemolytic component of honeybee venom, is unfolded in an aqueous environment and folds into an alpha-helical conformation in a lipid environment. Membrane fluidity is known to affect the activity and structure of melittin. By combining two structurally sensitive optical methods, circular dichroism (CD) and deep-ultraviolet resonance Raman spectroscopy (dUVRR), we have identified distinct structural fluctuations in melittin correlated with increased and decreased 1,2-dimyristoylsn-glycero-3-phosphocholine bilayer fluidities. CD spectra have reduced intensity at temperatures above 22 degrees C and high concentrations of the cholesterol analog 5-alpha-cholestan-3 beta-ol indicating distortions in the a-helical structure under these conditions. No increase in the amide S is observed in the temperature-dependent dUVRR spectra, suggesting an increase in 3(10)-helical structure with increasing temperatures above 22 degrees C. However, incorporation of 25 mol% 5 alpha-cholestan-3 beta-ol resulted in a small increase in the amide S intensity indicating partial unfolding of melittin. (C) 2014 Wiley Periodicals, Inc.
引用
收藏
页码:895 / 902
页数:8
相关论文
共 57 条
  • [1] Alteration in membrane fluidity and lipid composition, and modulation of H+-ATPase activity in Saccharomyces cerevisiae caused by decanoic acid
    Alexandre, H
    Mathieu, B
    Charpentier, C
    [J]. MICROBIOLOGY-SGM, 1996, 142 : 469 - 475
  • [2] Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin
    Almen, Markus Sallman
    Nordstrom, Karl J. V.
    Fredriksson, Robert
    Schioth, Helgi B.
    [J]. BMC BIOLOGY, 2009, 7 : 50
  • [3] The membrane-induced structure of melittin is correlated with the fluidity of the lipids
    Andersson, August
    Biverstahl, Henrik
    Nordin, Jon
    Danielsson, Jens
    Lindahl, Emma
    Maler, Lena
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2007, 1768 (01): : 115 - 121
  • [4] Armen R, 2003, PROTEIN SCI, V12, P1145, DOI 10.1110/ps.0240103
  • [5] Biophysical approaches to membrane protein structure determination
    Arora, A
    Tamm, LK
    [J]. CURRENT OPINION IN STRUCTURAL BIOLOGY, 2001, 11 (05) : 540 - 547
  • [6] Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    Arrondo, JLR
    Goñi, FM
    [J]. PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 1999, 72 (04) : 367 - 405
  • [7] Dihedral ψ angle dependence of the amide III vibration:: A uniquely sensitive UV resonance Raman secondary structural probe
    Asher, SA
    Ianoul, A
    Mix, G
    Boyden, MN
    Karnoup, A
    Diem, M
    Schweitzer-Stenner, R
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2001, 123 (47) : 11775 - 11781
  • [8] Austin J.C., 1993, Adv. Spectrosc, V20, P55
  • [9] MELITTIN BOUND TO DODECYLPHOSPHOCHOLINE MICELLES H-1-NMR ASSIGNMENTS AND GLOBAL CONFORMATIONAL FEATURES
    BROWN, LR
    WUTHRICH, K
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1981, 647 (01) : 95 - 111
  • [10] Observation of persistent -helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep-UV resonance Raman spectroscopy
    Brown, Mia C.
    Mutter, Andrew C.
    Koder, Ronald L.
    JiJi, Renee D.
    Cooley, Jason W.
    [J]. JOURNAL OF RAMAN SPECTROSCOPY, 2013, 44 (07) : 957 - 962