Identification of a second membrane‐active 13‐residue peptide segment in the antimicrobial protein, bovine seminalplasmin

Sitaram, N.; Subbalakshmi, Chilukuri; Nagaraj, Ramakrishnan

doi:10.1016/0014-5793(93)80935-n

Cited by 11 publications

(5 citation statements)

References 28 publications

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“…The peptide is more active than the other earlier described active shorter synthetic segments of SPLN, SPF [17] and SLS [19]. In fact, the potency against E. coli is comparable to that of SPLN.…”

Section: Resultsmentioning

confidence: 74%

Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin

et al. 1997

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Seminalplasmin (SPLN) is a 47-residue protein isolated from bovine seminal plasma having potent antimicrobial activity against a broad spectrum of microorganisms. SPLN, also known as caltrin, acts as a calcium transport regulator in bovine sperms. Analysis of the sequence of SPLN reveals a 27-residue stretch with the sequence SLSRYAKLANRLANPKL-LETFLSKWIG more hydrophobic than the rest of the protein. It is demonstrated that a synthetic peptide corresponding to this 27-residue segment has antimicrobial activity comparable to that of SPLN. It does not exhibit hemolytic activity at concentrations where antibacterial activity is observed. Since P27 can be conveniently obtained in large amounts by chemical synthesis, it could serve not only as a starting compound to obtain peptides with improved antibacterial activity but also to understand the role of SPLN in reproductive physiology.

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Section: Resultsmentioning

confidence: 74%

Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin

et al. 1997

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“…Such segments play an important role in the biological activities of several antimicrobial/lytic peptides. Short synthetic peptide, encompassing ‘surface seeking' segments have been shown to exhibit antimicrobial and hemolytic activities [6–8, 11, 30–32]. Thus, it was interesting to see whether a synthetic peptide corresponding to C‐terminal 12–26 segment of melittin, encompassing its most amphiphilic region, also possesses biological activity.…”

Section: Discussionmentioning

confidence: 99%

“…The emergence of microbes that are resistant to conventionally used antibiotics has triggered considerable interest in the structure‐function relationship studies in short antimicrobial peptides in recent years [1]. In addition to naturally occurring short antimicrobial peptides like indolicidin, protegrins and tachyplesins, shorter segments of comparatively larger peptides and proteins like seminalplasmin, cecropins, neuropeptide Y, dermaseptins and lactoferrin have been studied in considerable detail [2–12]. These studies are aimed at not only delineating the structural requirements for selective antimicrobial activity but also to develop peptides that could have potential as therapeutic agents.…”

Section: Introductionmentioning

confidence: 99%

Biological activities of C‐terminal 15‐residue synthetic fragment of melittin: design of an analog with improved antibacterial activity

1999

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Melittin, the 26-residue predominant toxic peptide from bee venom, exhibits potent antibacterial activity in addition to its hemolytic activity. The synthetic peptide of 15 residues corresponding to its C-terminal end (MCF), which encompasses its most amphiphilic segment, is now being shown to possess antibacterial activity about 5^7 times less compared to that of melittin. MCF, however, is 300 times less hemolytic. An analog of MCF, MCFA, in which two cationic residues have been transpositioned to the N-terminal region from the C-terminal region, exhibits antibacterial activity comparable to that of melittin, but is only marginally more hemolytic than MCF. The biophysical properties of the peptides, like folding and aggregation, correlate well with their biological properties.z 1999 Federation of European Biochemical Societies.

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“…10, it was noted that, in the presence of trifluoroethanol, the helical structure of the synthetic peptide was strongly induced. Recently, a 13-residue peptide bearing antimicrobial activity was identified in bovine seminalplasmin (Sitaram et al, 1993) which indicates that a short fragment of only 13 residues which can adopt an amphiphilic helical structure is able to exhibit antimicrobial activity.…”

Section: Structural Features Of Cgbmentioning

confidence: 99%

Processing of Chromogranin B in Bovine Adrenal Medulla. Identification of Secretolytin, the Endogenous C-Terminal Fragment of Residues 614-626 with Antibacterial Activity

Strub¹,

Garcia-Sablone²,

Lønning³

et al. 1995

Eur J Biochem

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Chromogranins constitute a family of acidic soluble proteins widely distributed in endocrine cells and neurons. Chromogranin A, the major soluble component in bovine adrenal medullary secretory granules in chromaffin cells, has been shown to be actively processed to peptide fragments [Metz-Boutigue, M. H., Garcia-Sablone, P., Hogue-Angeletti, R. & Aunis, D. (1993) Eur. J. Biochem. 217, 247-2571. In the present paper, the structural features of the proteolytic degradation mechanism of chromogranin B/ secretogranin I have been characterized with regard to the possible function of this protein as a precursor of biologically active peptides.Chromogranin-B-derived fragments present in bovine chromafh granules were identified by microsequencing after separation by two-dimensional gel electrophoresis or high-performance liquid chromatography. A similar approach was performed to characterize chromogranin-B-derived fragments released into the extracellular space from depolarized bovine cultured chromaffin cells. In chromogranin B, 18 cleavage sites were identified along the protein chain and chromogranin Bhecretogranin I fragments were generated by proteolytic attack at both the N-terminus and C-terminus.A major fragment corresponding to residues 614-626 of the C-terminal sequence, was identified in the extracellular space; this peptide was found to share sequence and structural similarities with the lytic domain of cecropins and, as expected from this similarity, to display potent antibacterial properties. Endogenous and synthetic peptides were active on Micrococcus luteus, killing bacteria in the micromolar concentration range. The synthetic peptide slows the growth of Bacillus megaterium and was inactive towards Escherichia coli. In addition, the synthetic peptide was unable to induce hemolytic activity. This antibacterial function might be of biological significance in the neuroendocrine system of living organisms. We propose to name this peptide secretolytin.

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Identification of a second membrane‐active 13‐residue peptide segment in the antimicrobial protein, bovine seminalplasmin

Cited by 11 publications

References 28 publications

Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin

Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin

Biological activities of C‐terminal 15‐residue synthetic fragment of melittin: design of an analog with improved antibacterial activity

Processing of Chromogranin B in Bovine Adrenal Medulla. Identification of Secretolytin, the Endogenous C-Terminal Fragment of Residues 614-626 with Antibacterial Activity

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