Studies of synthetic peptide analogs of the amphipathic helix. Effect of charged amino acid residue topography on lipid affinity.

KANELLIS, P.; Romans, Alice Y.; Johnson, B J; Kercret, Henri; Chiovetti, Robert; Allen, Theresa M.; Segrest, Jere P.

doi:10.1016/s0021-9258(19)70314-7

Cited by 92 publications

(28 citation statements)

References 29 publications

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“…For both forms of the peptide, the remainder of the structure seems to be largely random with <10% /3-sheet structure, by comparison to the reference poly lysine spectra of Greenfield and Fasman (1969). Similar estimations for percentage helicity were obtained for other membrane-binding amphipathic peptides: a peptide derived from the N-terminal region of influenza hemagglutinin was 45% helical (Lear & DeGrado, 1987); model ion-channel peptides were 60-70% helical (Agawa et al, 1991;Chung et al, 1992); and peptides modeled from apolipoproteins were up to ~50% helical (Kanellis et al, 1980;Anantharamaiah et al, 1985;Epand et al, 1987;Yoshimura et al, 1992).…”

Section: Discussionsupporting

confidence: 58%

“…Thus, there would be two populations of peptide, bound and unbound, which would be exchanging. This was also evident in the case of a synthetic model amphipathic peptide where not all of the peptide was tightly associated with the lipid vesicles in a density gradient ultracentifugation (Kanellis et al, 1980). A Portion of the Peptide Intercalates into the Hydrophobic Core of the Membrane.…”

Section: Discussionmentioning

confidence: 88%

“…Synthetic peptides have previously been used to study the membrane interactions of the proposed N-terminal binding region of influenza hemagluttinin (Lear & Degrado, 1987;Claque et al, 1991), the putative anionic lipid-binding region of the erythrocyte Ca2+ pump (Filoteo et al, 1992), N-terminal signal sequences (Killian etal., 1990;McKnight et al, 1991), peptides derived from ion-channel proteins (Agawa et al, 1991;Chung et al, 1992), and other peptides which model the amphipathic helical structure (Kanellis et al, 1980;Anantharamaiah et al, 1985;Epand et al, 1987).…”

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confidence: 99%

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Membrane-Binding Amphipathic .alpha.-Helical Peptide Derived from CTP:Phosphocholine Cytidylyltransferase

Johnson

Cornell²

1994

Biochemistry

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A peptide corresponding to a portion of the amphipathic alpha-helical region of CTP:phosphocholine cytidylyltransferase was synthesized. This region of the enzyme was proposed to be the membrane-binding domain [Kalmar, G.B., Kay, R.J., Lachance, A., Aebersold, R., & Cornell, R.B. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 6029]. We have shown that the peptide is physically associated with PG vesicles. CD of the peptide in buffer suggested a primarily random structure, while, in the presence of trifluoroethanol, the peptide was alpha-helical. Anionic lipid vesicles promoted an alpha-helical conformation, whereas neutral or cationic lipid vesicles did not alter the random structure of the peptide, suggesting a selective stabilization of the alpha-helix by anionic membranes. The fluorescence of the single tryptophan residue, which lies on the hydrophobic face of the amphipathic alpha-helix, was studied. Anionic lipid vesicles specifically induced a shift in the fluorescence to a lower wavelength. Fluorescence quenching by the aqueous-phase quencher, I-, and the lipid-phase quencher 9,10-dibromo-PC was used to determine the accessibility of the tryptophan to each of these environments. The presence of anionic lipid vesicles, but not nonanionic lipid vesicles, decreased the quenching by I- suggesting that, in the presence of anionic lipids, the tryptophan residue is poorly accessible to the aqueous I-. Dibromo-PC significantly quenched the fluorescence only when present in anionic vesicles, confirming the membrane location of the tryptophan residue and the lipid specificity of this interaction.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionsupporting

confidence: 58%

Section: Discussionmentioning

confidence: 88%

mentioning

confidence: 99%

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Membrane-Binding Amphipathic .alpha.-Helical Peptide Derived from CTP:Phosphocholine Cytidylyltransferase

Johnson

Cornell²

1994

Biochemistry

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“…The nanofiber formation between the gel-phase lipid and the peptide was likely to be kinetically inhibited by the high energetic cost of inserting the amphipathic peptide into the rigid gel-phase bilayers. Similar interactions dependent on the lipid bilayer phase have been observed in the formation of lipid–peptide nanodiscs. , …”

Section: Resultssupporting

confidence: 69%

“…Similar interactions dependent on the lipid bilayer phase have been observed in the formation of lipid−peptide nanodiscs. 21,22 A large CD spectral change was observed when the temperature was changed from 25 to 37 °C, suggesting a higher transition temperature than that of the DLPC-and DMPC−18A[A11C] mixtures. In addition to the CD spectra, the tryptophan fluorescence spectra of the DPPC−18A[A11C] and DLPC−18A[A11C] mixtures showed similar spectral shapes in the fibrillar state at 4 °C (Figure 6).…”

Section: Concentration-dependent Formation and Dissociation Of Popc−1...mentioning

confidence: 99%

Amphipathic Peptide–Phospholipid Nanofibers: Phospholipid Specificity and Dependence on Concentration and Temperature

et al. 2021

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The design of nanoassemblies is an important part of the development of new materials for applications in nanomedicine and biosensors. In our previous study, cysteine substitution of the apolipoprotein A-I-derived peptide 18A at residue 11, 18A[A11C], bound to 1-palmitoyl-2-oleoylphosphatidylcholine to form fibrous aggregates at a lipid-to-peptide molar ratio of ≤2 and a fiber diameter of 10–20 nm. However, the mechanisms underlying the lipid–peptide interactions that enable nanofiber formation remain unclear. Here, we evaluated the phospholipid specificity, concentration dependence, and temperature dependence of the formation of 18A[A11C]–lipid nanofibers. Nanofibers were found to form in the presence of specific phospholipids and have a constant lipid/peptide stoichiometry of 1.2 ± 0.2. Moreover, an increase in the length of the acyl chain in phosphatidylcholines was found to increase the structural stability of the nanofibers. These results indicate that specific molecular interactions between peptides and both the headgroups and acyl chains of phospholipids are involved in nanofiber formation. Furthermore, the formation and disassembly of the nanofibers were reversibly controlled by changes in temperature and concentration. The results of the present study provide an insight into the creation of nanoassembling structures.

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Behavior of amphipathic helices on analysis via matrix methods, with application to glucagon, secretin, and vasoactive intestinal peptide

1983

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SynopsisA configuration partition function, which incorporates concepts embodied in the amphipathic helix hypothesis, has been formulated for a polypeptide in the presence of zwitterionic phospholipid. An enhanced probability is assigned to helix formation in any region of the polypeptide chain where side chains bearing charges of opposite sign will be situated on the same side of the a-helix but displaced from one another by one turn. This situation will arise when residues i -4 (or i -3) and i bear charges of opposite sign and residues i -4 (or i -3) through i are in a helical state. Illustrative calculations are performed for polypeptide chains in which the generalized nonionic amino acid residue serving as host has Zimm-Bragg parameters of o = lo-*, s = l. These calculations define conditions under which two interacting charged pairs can cooperate in a synergistic helix augmentation even when the two pairs are separated by significantly more than four generalized nonionic amino acid residues. Furthermore, the two interacting charged pairs, as well as the intervening amino acid residues, may become helical as one unit. Significant augmentation in helicity is observed with plausible values for the enhanced probability assigned to helix formation for an interacting pair. This model predicts correctly that glucagon and secretin, but not vasoactive intestinal peptide, undergo a coil-to-helix transition in the presence of zwitterionic phospholipid. This prediction is made with plausible values for the parameter used to express the helicity enhancement. The experimental observation with zwitterionic phospholipids is the direct opposite of that seen for these three peptides in the presence of anionic lipids and detergents. In anionic lipids the amount of induced helicity is in the following order: glucagon < secretin < vasoactive intestinal peptide. Results obtained with these three peptides demonstrate that the nature of the head group of the lipid is important for lipid-protein interaction and that the resulting conformational changes can be rationalized by matrix methods.

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Studies of synthetic peptide analogs of the amphipathic helix. Effect of charged amino acid residue topography on lipid affinity.

Cited by 92 publications

References 29 publications

Membrane-Binding Amphipathic .alpha.-Helical Peptide Derived from CTP:Phosphocholine Cytidylyltransferase

Membrane-Binding Amphipathic .alpha.-Helical Peptide Derived from CTP:Phosphocholine Cytidylyltransferase

Amphipathic Peptide–Phospholipid Nanofibers: Phospholipid Specificity and Dependence on Concentration and Temperature

Behavior of amphipathic helices on analysis via matrix methods, with application to glucagon, secretin, and vasoactive intestinal peptide

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