Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II

Park, Tae Joo; Kim, Jisun; Ahn, Hee‐Chul; Kim, Yongae

doi:10.1016/j.bpj.2011.06.067

Cited by 23 publications

(22 citation statements)

References 32 publications

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“…Recently, in an attempt to overcome sepsis and other diseases caused by Gram-negative bacteria, the application of AMPs to new agents has been attracting much attention. Many reports have analyzed the structures of AMPs in the presence of LPS or mimetic membrane of Gram-negative bacteria to understand the mechanism of LPS or lipid-membrane recognition in AMPs [37][38][39]. However, the details of the interaction between AMPs and LPS and the relationship between the mechanisms of LPS recognition and structures of AMPs have not yet been revealed.…”

Section: Discussionmentioning

confidence: 99%

Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide

Kushibiki

Kamiya

Aizawa

et al. 2014

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Lipopolysaccharide (LPS) is a major constituent of the outer membrane of Gram-negative bacteria and is the very first site of interactions with antimicrobial peptides (AMPs). In order to gain better insight into the interaction between LPS and AMPs, we determined the structure of tachyplesin I (TP I), an antimicrobial peptide derived from horseshoe crab, in its bound state with LPS and proposed the complex structure of TP I and LPS using a docking program.CD and NMR measurements revealed that binding to LPS slightly extends the two β-strands of TP I and stabilizes the whole structure of TP I. The fluorescence wavelength of an intrinsic tryptophan of TP I and fluorescence quenching in the presence or absence of LPS indicated that a tryptophan residue is incorporated into the hydrophobic environment of LPS. Finally, we succeeded in proposing a structural model for the complex of TP I and LPS by using a docking program. The calculated model structure suggested that the cationic residues of TP I interact with phosphate groups and saccharides of LPS, whereas hydrophobic residues interact with the acyl chains of LPS.

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Section: Discussionmentioning

confidence: 99%

Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide

Kushibiki

Kamiya

Aizawa

et al. 2014

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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“…B). Such large chemical shift differences have been observed between a random coil peptide and its DPC micelle‐bound state with a helical structure . Moreover, the NOE cross‐peaks were rather limited in the DPC‐free buffer but strongly increased upon the addition of DPC micelles, indicating that binding to micelles induces CCR2 Pro‐C folding (Fig.…”

Section: Resultsmentioning

confidence: 77%

Structural basis for the binding of the membrane‐proximal C‐terminal region of chemokine receptor CCR2 with the cytosolic regulator FROUNT

et al. 2014

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C region to a cytosolic regulator has not been structurally analyzed. The chemokine receptor CCR2 is a member of the GPCR superfamily, and the Pro-C region of CCR2 binds to the cytosolic regulator FROUNT. Studying the interaction between CCR2 Pro-C and FROUNT at an atomic level provides a basis for understanding the signal transduction mechanism via GPCRs. NOE-based NMR experiments showed that, when bound to FROUNT, CCR2 Pro-C adopted a helical conformation, as well as when embedded in dodecylphosphocholine micelles. A comparison of two types of cross-saturation-based NMR experiments, applied to a three-component mixture of Pro-C, FROUNT and micelles or a two-component mixture of Pro-C and micelles, revealed that the hydrophobic binding surface on Pro-C for FROUNT mostly overlapped with the binding site for micelles, suggesting competitive binding of Pro-C between FROUNT and micelles. Leu316 was important for both FROUNT and micelle binding. Phe319 was newly identified to be crucial for FROUNT binding, by NMR and mutational analyses. The association and dissociation rates of CCR2 Pro-C for lipid bilayer biomembranes were faster than those for FROUNT. We previously reported that FROUNT binding to CCR2 is detectable even in unstimulated cells and increases in response to chemokine stimulation. Taken together, these results support a model of CCR2 equilibrium: chemokine binding changes the conformational equilibrium of CCR2 toward the active state, and Pro-C switches its binding partner from the membrane to FROUNT. Structured digital abstractFROUNT binds to CCR2 Pro-C by surface plasmon resonance (1, 2) FROUNT and CCR2 Pro-C bind by nuclear magnetic resonance (View interaction)

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“…Lactophoricin (LPcin) is separated from bovine milk and is a good candidate for a cationic amphipathic AMP, consisting of 23 amino acids [20][21][22]. The N-terminal 6 amino acids truncated variant of LPcin has been confirmed in previous experiments to have no antibiotic activity [23]. In this paper, the 11 peptide analogs in Table 1 and Fig.…”

Section: Introductionmentioning

confidence: 76%

Design, Characterization, and Antimicrobial Activity of a Novel Antimicrobial Peptide Derived from Bovine Lactophoricin

Kim¹,

Joeng²,

Kim³

2017

Journal of Microbiology and Biotechnology

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Lactophoricin (LPcin), which is a part of proteose peptone isolated from bovine milk, is a cationic amphipathic α-helical antimicrobial peptide. Its truncated variants and mutated analogs were designed and their antimicrobial activities were evaluated by using various assays, like broth dilution methods and disk diffusion methods as well as hemolysis assay. Three analogs, LPcin-C8 (LPcin-YK1), LPcin-T2&6W (LPcin-YK2), and LPcin-T2&6W-C8 (LPcin-YK3), which showed better antibiotic activities than LPcin, were selected. Their secondary structures were also characterized by using CD spectropolarimetry. These three analogs of LPcin could be used as an alternative source of powerful antibacterial agents.

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Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II

Cited by 23 publications

References 32 publications

Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide

Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide

Structural basis for the binding of the membrane‐proximal C‐terminal region of chemokine receptor CCR2 with the cytosolic regulator FROUNT

Design, Characterization, and Antimicrobial Activity of a Novel Antimicrobial Peptide Derived from Bovine Lactophoricin

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