The Use of Dodecylphosphocholine Micelles in Solution NMR

Kallick, Deborah A.; Tessmer, Michael R.; Watts, Charles R.; Li, Ching-Yuan

doi:10.1006/jmrb.1995.1146

Cited by 148 publications

(213 citation statements)

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“…Our studies indicate that the peptide adopts its structure at a lipid: peptide ratio of 9:1, and maintains this structure throughout the addition of DODPC to a lipid:peptide ratio of 50:1. This is in agreement with studies of peptides of this size previously reported [20]. The expansion of the amide region of NOESY spectra in Fig.…”

Section: Comparison Of High and Low Lipid Concentrationsupporting

confidence: 93%

“…All rights reserved. P//S0014-5793 (9 7)01113-7 be with a lipid:peptide of 9:1, consistent with conditions for dynorphin A [20]. Additionally, we have carried out NMR NOESY experiments at higher lipid concentration with a lipid: peptide of 50:1.…”

Section: Introductionsupporting

confidence: 70%

“…There are disadvantages to using higher lipid concentrations. The aggregation number of the micelles increases with lipid concentration [20], resulting in increased line widths.…”

Section: Discussionmentioning

confidence: 99%

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A cytoplasmic peptide of the neurotrophin receptor p75NTR: induction of apoptosis and NMR determined helical conformation

et al. 1997

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The neurotrophin receptor (NTR) and tumor necrosis factor receptor family of receptors regulate apoptotic cell death during development and in adult tissues [Beutler and van Huffel, Science 264 (1994) 667-668]. We have examined a fragment of p75NTR from the carboxyl terminus of the receptor and a variant form of this peptide via NMR techniques and in vitro assays for apoptotic activity. The wild type peptide induces apoptosis and adopts a helical conformation oriented parallel to the surface of lipid micelles, whereas the variant form adopts a non-helical conformation in the presence of lipid and shows no activity. These experiments suggest a link between structure and function of the two peptides.

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Section: Comparison Of High and Low Lipid Concentrationsupporting

confidence: 93%

Section: Introductionsupporting

confidence: 70%

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A cytoplasmic peptide of the neurotrophin receptor p75NTR: induction of apoptosis and NMR determined helical conformation

et al. 1997

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“…DPC has been commonly used as a mimetic membrane study model in solution NMR ( 47 ). Undeuterated DPC of 3 mM concentration was added to isotopically labeled protein premixed with 2 mM of SA U44069 or PA 12415.…”

Section: L-pgds Interactions With Dedecylphosphocholine To Model Membmentioning

confidence: 99%

Structural and dynamic insights into substrate binding and catalysis of human lipocalin prostaglandin D synthase

Lim

Chen

Teo

et al. 2013

Journal of Lipid Research

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“…Thus, a conformational change upon membrane association may play a crucial role in the function of antimicrobial peptides, but the experimental difficulties inherent in studying this change are considerable (10). The interior of a detergent micelle reasonably mimics the environment at the interior of a phospholipid bilayer (11,12). Amphiphilic peptides readily associate with micelles in aqueous buffer and acquire rotational correlation times comparable to those of 20-25 kDa proteins.…”

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confidence: 99%

Solution and Micelle-Bound Structures of Tachyplesin I and Its Active Aromatic Linear Derivatives^,

2002

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Tachyplesin I is a 17-residue peptide isolated from the horseshoe crab, Tachyplesus tridentatus. It has high antimicrobial activity and adopts a β-hairpin conformation in solution stabilized by two cross-strand disulfide bonds. We report an NMR structural investigation of wild-type tachyplesin I and three linear derivatives (denoted TPY4, TPF4, and TPA4 in which the bridging cysteine residues are uniformly replaced with tyrosine, phenylalanine, and alanine, respectively). The three-dimensional aqueous solution structures of the wild type and the active variant TPY4 reveal very similar β-hairpin conformations. In contrast, the inactive variant TPA4 is unstructured in solution. The arrangement of the tyrosine side chains in the TPY4 structure suggests that the β-hairpin is stabilized by aromatic ring stacking interactions. This is supported by experiments in which the β-hairpin structure of TPF4 is disrupted by the addition of phenol, but not by the addition of an equimolar amount of cyclohexanol. We have also determined the structures of wild-type tachyplesin I and TPY4 in the presence of dodecylphosphocholine micelles. Both peptides undergo significant conformational rearrangement upon micelle association. Analysis of the micelle-associated peptide structures shows an increased level of exposure of specific hydrophobic side chains and an increased hydrophobic integy moment. Comparison of the structures in micelle and aqueous solution for both wildtype tachyplesin I and TPY4 reveals two requirements for high antimicrobial activity: a β-hairpin fold in solution and the ability to rearrange critical side chain residues upon membrane association. ReceiVed May 23, 2002; ReVised Manuscript ReceiVed August 17, 2002 ABSTRACT: Tachyplesin I is a 17-residue peptide isolated from the horseshoe crab, Tachyplesus tridentatus. It has high antimicrobial activity and adopts a -hairpin conformation in solution stabilized by two crossstrand disulfide bonds. We report an NMR structural investigation of wild-type tachyplesin I and three linear derivatives (denoted TPY4, TPF4, and TPA4 in which the bridging cysteine residues are uniformly replaced with tyrosine, phenylalanine, and alanine, respectively). The three-dimensional aqueous solution structures of the wild type and the active variant TPY4 reveal very similar -hairpin conformations. In contrast, the inactive variant TPA4 is unstructured in solution. The arrangement of the tyrosine side chains in the TPY4 structure suggests that the -hairpin is stabilized by aromatic ring stacking interactions. This is supported by experiments in which the -hairpin structure of TPF4 is disrupted by the addition of phenol, but not by the addition of an equimolar amount of cyclohexanol. We have also determined the structures of wild-type tachyplesin I and TPY4 in the presence of dodecylphosphocholine micelles. Both peptides undergo significant conformational rearrangement upon micelle association. Analysis of the micelle-associated peptide structures shows an increased level of expo...

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The Use of Dodecylphosphocholine Micelles in Solution NMR

Cited by 148 publications

References 0 publications

A cytoplasmic peptide of the neurotrophin receptor p75NTR: induction of apoptosis and NMR determined helical conformation

A cytoplasmic peptide of the neurotrophin receptor p75NTR: induction of apoptosis and NMR determined helical conformation

Structural and dynamic insights into substrate binding and catalysis of human lipocalin prostaglandin D synthase

Solution and Micelle-Bound Structures of Tachyplesin I and Its Active Aromatic Linear Derivatives^,

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The Use of Dodecylphosphocholine Micelles in Solution NMR

Cited by 148 publications

References 0 publications

A cytoplasmic peptide of the neurotrophin receptor p75NTR: induction of apoptosis and NMR determined helical conformation

A cytoplasmic peptide of the neurotrophin receptor p75NTR: induction of apoptosis and NMR determined helical conformation

Structural and dynamic insights into substrate binding and catalysis of human lipocalin prostaglandin D synthase

Solution and Micelle-Bound Structures of Tachyplesin I and Its Active Aromatic Linear Derivatives,

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Solution and Micelle-Bound Structures of Tachyplesin I and Its Active Aromatic Linear Derivatives^,