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Esben Skipper Sørensen

Proteolytic activation of proteose peptone component 3 by release of a C-terminal peptide with antibacterial properties

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Proteolytic activation of proteose peptone component 3 by release of a C-terminal peptide with antibacterial properties. / Pedersen, Lise Refstrup Linnebjerg; Hansted, J.G.; Nielsen, Søren Bang; Petersen, T.E.; Sørensen, U.S.; Otzen, D.; Sørensen, E.S.

In: Journal of Dairy Science, Vol. 95, No. 6, 01.06.2012, p. 2819-2829.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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@article{bc6b8288221d437dbc9fd1d53fbe5b40,
title = "Proteolytic activation of proteose peptone component 3 by release of a C-terminal peptide with antibacterial properties",
abstract = "The milk protein proteose peptone component 3 (PP3, also known as lactophorin) is a small phosphoglycoprotein, which is exclusively expressed in the lactating mammary gland. A 23-residue synthetic peptide (lactophoricin, Lpcin S), corresponding to the C-terminal amphipathic α-helix of PP3, has previously been shown to permeabilize membranes and display antibacterial activity. Lactophorin readily undergoes proteolytic cleavage in milk and during dairy processing, and it has been suggested that PP3-derived peptides are part of milk's endogenous defense system against bacteria. Here, we report that a 26-residue C-terminal peptide (Lpcin P) can be generated by trypsin proteolysis of PP3 and that structural and functional studies of Lpcin P indicate that the peptide has antibacterial properties. The Lpcin P showed α-helical structure in both anionic and organic solvents, and the amount of α-helical structure was increased in the presence of lipid vesicles. Oriented circular dichroism showed that Lpcin P oriented parallel to the membrane surface. However, the peptide permeabilized calcein-containing vesicles efficiently. Lpcin P displayed antibacterial activity against Streptococcus thermophilus, but not against Staphylococcus aureus and Escherichia coli. The PP3 full-length protein did not display the same properties, which could indicate that PP3 functions as a precursor protein that upon proteolysis, releases a bioactive antibacterial peptide.",
author = "Pedersen, {Lise Refstrup Linnebjerg} and J.G. Hansted and Nielsen, {S{\o}ren Bang} and T.E. Petersen and U.S. S{\o}rensen and D. Otzen and E.S. S{\o}rensen",
note = "MEDLINE{\textregistered} is the source for the MeSH terms of this document.",
year = "2012",
month = jun,
day = "1",
doi = "10.3168/jds.2011-4837",
language = "English",
volume = "95",
pages = "2819--2829",
journal = "Journal of Dairy Science",
issn = "0022-0302",
publisher = "Elsevier Inc.",
number = "6",

}

RIS

TY - JOUR

T1 - Proteolytic activation of proteose peptone component 3 by release of a C-terminal peptide with antibacterial properties

AU - Pedersen, Lise Refstrup Linnebjerg

AU - Hansted, J.G.

AU - Nielsen, Søren Bang

AU - Petersen, T.E.

AU - Sørensen, U.S.

AU - Otzen, D.

AU - Sørensen, E.S.

N1 - MEDLINE® is the source for the MeSH terms of this document.

PY - 2012/6/1

Y1 - 2012/6/1

N2 - The milk protein proteose peptone component 3 (PP3, also known as lactophorin) is a small phosphoglycoprotein, which is exclusively expressed in the lactating mammary gland. A 23-residue synthetic peptide (lactophoricin, Lpcin S), corresponding to the C-terminal amphipathic α-helix of PP3, has previously been shown to permeabilize membranes and display antibacterial activity. Lactophorin readily undergoes proteolytic cleavage in milk and during dairy processing, and it has been suggested that PP3-derived peptides are part of milk's endogenous defense system against bacteria. Here, we report that a 26-residue C-terminal peptide (Lpcin P) can be generated by trypsin proteolysis of PP3 and that structural and functional studies of Lpcin P indicate that the peptide has antibacterial properties. The Lpcin P showed α-helical structure in both anionic and organic solvents, and the amount of α-helical structure was increased in the presence of lipid vesicles. Oriented circular dichroism showed that Lpcin P oriented parallel to the membrane surface. However, the peptide permeabilized calcein-containing vesicles efficiently. Lpcin P displayed antibacterial activity against Streptococcus thermophilus, but not against Staphylococcus aureus and Escherichia coli. The PP3 full-length protein did not display the same properties, which could indicate that PP3 functions as a precursor protein that upon proteolysis, releases a bioactive antibacterial peptide.

AB - The milk protein proteose peptone component 3 (PP3, also known as lactophorin) is a small phosphoglycoprotein, which is exclusively expressed in the lactating mammary gland. A 23-residue synthetic peptide (lactophoricin, Lpcin S), corresponding to the C-terminal amphipathic α-helix of PP3, has previously been shown to permeabilize membranes and display antibacterial activity. Lactophorin readily undergoes proteolytic cleavage in milk and during dairy processing, and it has been suggested that PP3-derived peptides are part of milk's endogenous defense system against bacteria. Here, we report that a 26-residue C-terminal peptide (Lpcin P) can be generated by trypsin proteolysis of PP3 and that structural and functional studies of Lpcin P indicate that the peptide has antibacterial properties. The Lpcin P showed α-helical structure in both anionic and organic solvents, and the amount of α-helical structure was increased in the presence of lipid vesicles. Oriented circular dichroism showed that Lpcin P oriented parallel to the membrane surface. However, the peptide permeabilized calcein-containing vesicles efficiently. Lpcin P displayed antibacterial activity against Streptococcus thermophilus, but not against Staphylococcus aureus and Escherichia coli. The PP3 full-length protein did not display the same properties, which could indicate that PP3 functions as a precursor protein that upon proteolysis, releases a bioactive antibacterial peptide.

UR - http://www.scopus.com/inward/record.url?scp=84862072352&partnerID=8YFLogxK

U2 - 10.3168/jds.2011-4837

DO - 10.3168/jds.2011-4837

M3 - Journal article

C2 - 22612919

AN - SCOPUS:84862072352

VL - 95

SP - 2819

EP - 2829

JO - Journal of Dairy Science

JF - Journal of Dairy Science

SN - 0022-0302

IS - 6

ER -