Solution Structure of a Designed Amphipathic Antimicrobial Synthetic Peptide, PGAa

Hong, Eunmi; Jeong, Pan Young; Jung, Jin; Kim, Yangmee; Cheong, Chaejoon; Paik, Young Ki; Lee, Weontae

doi:10.1006/bbrc.2000.3587

Cited by 2 publications

(3 citation statements)

References 27 publications

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“…chloroform/methanol and trifluoroethanol/water, respectively. This is in agreement with other studies comparing peptide structures in trifluoroethanol-, chloroform-and micelle-containing solutions [35][36][37][38][39][40], where trifluoroethanol was also found to induce the highest content of a helical secondary structure.…”

Section: R E S U L T S a N D Discussionsupporting

confidence: 93%

“…Sequences were obtained from the SwissProt data bank. (34)(35)(36)(37)(38)(39)(40)(41)(42)(43)(44)(45)(46)(47)(48)(49)(50)(51) peptide in presence of 100 mM dodecyl-PCho is shown as surface representation from three different views, rotated by 120 degrees against each other. Orientation of the peptide is N-terminal to the top.…”

Section: R E S U L T S a N D Discussionmentioning

confidence: 99%

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Structure of human immunodeficiency virus type 1 Vpr(34–51) peptide in micelle containing aqueous solution

Engler

Stangler

Willbold

2002

European Journal of Biochemistry

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Human immunodeficiency virus type 1 protein R (HIV-1 Vpr) promotes nuclear entry of viral nucleic acids in nondividing cells, causes G 2 cell cycle arrest and is involved in cellular differentiation and cell death. Vpr subcellular localization is as variable as its functions. It is known, that consistent with its role in nuclear transport, Vpr localizes to the nuclear envelope of human cells. Further, a reported ion channel activity of Vpr is clearly dependent on its localization in or at membranes. We focused our structural studies on the secondary structure of a peptide consisting of residues 34-51 of HIV-1 Vpr. This part of Vpr plays an important role in Vpr oligomerization, contributes to cell cycle arrest activity, and is essential for virion incorporation and binding to HHR23A, a protein involved in DNA repair. Employing NMR spectroscopy we found this part of Vpr to be almost completely a helical in the presence of micelles, as well as in trifluoroethanol containing and methanol/ chloroform solvent. Our results provide structural data suggesting residues 34-51 of Vpr to contain an amphipathic, leucine-zipper-like a helix, which serves as a basis for oligomerization of Vpr and its interactions with cellular and viral factors involved in subcellular localization and virion incorporation of Vpr.

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Section: R E S U L T S a N D Discussionsupporting

confidence: 93%

Section: R E S U L T S a N D Discussionmentioning

confidence: 99%

Structure of human immunodeficiency virus type 1 Vpr(34–51) peptide in micelle containing aqueous solution

Engler

Stangler

Willbold

2002

European Journal of Biochemistry

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“…[22][23][24][25] Like exchangeable apolipoproteins, the synuclein sequences are characterized by the presence of a set of imperfect 11-residue repeats. On the basis of this 11-mer periodicity, Segrest et al have suggested the possibility that apolipoprotein A-I forms an 11/3 helix with a pitch of 3 turns per 11 residues.…”

Section: Discussionmentioning

confidence: 99%

The 11‐mer repeats of human α‐synuclein in vesicle interactions and lipid composition discrimination: A cooperative role

Bisaglia¹,

Schievano²,

Caporale³

et al. 2006

Biopolymers

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alpha-Synuclein is a protein abundant in presynaptic terminals in the brain. The N-terminal region of the sequence contains an imperfect 11-residue periodicity also found in A-class apolipoproteins and able to fold into an amphipathic helix. Here, the ability of three fragments of the protein, which include one, two, and all repeats, respectively, to bind to vesicles of different phospholipid composition is described. The results suggest a cooperative action of the repeats in selecting target membranes for interaction based on their lipid composition. This deduction is possibly related to the physiological role of the protein, which is still poorly understood.

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Solution Structure of a Designed Amphipathic Antimicrobial Synthetic Peptide, PGAa

Cited by 2 publications

References 27 publications

Structure of human immunodeficiency virus type 1 Vpr(34–51) peptide in micelle containing aqueous solution

Structure of human immunodeficiency virus type 1 Vpr(34–51) peptide in micelle containing aqueous solution

The 11‐mer repeats of human α‐synuclein in vesicle interactions and lipid composition discrimination: A cooperative role

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