Literature DB >> 16261252

Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties.

J L Gifford1, H N Hunter, H J Vogel.   

Abstract

The peptide lactoferricin (Lfcin) can be released from the multifunctional protein lactoferrin (LF) through proteolysis by pepsin under acidic conditions, a reaction that occurs naturally in the stomach. Lfcin encompasses a large portion of the functional domain of the intact protein, and in many cases it not only retains the activities of LF but is more active. Lfcin possesses strong antimicrobial and weak antiviral activities, and it also has potent antitumor and immunological properties. This review covers the current state of research in this field, focusing on the many beneficial activities of this peptide. Throughout we will discuss the breadth of Lfcin activity as well as the mechanism of action. Many recent studies have drawn attention to the fact that the main site of action for the peptide may be intracellular. In addition the results of structural and dynamic studies of Lfcin are presented, and the relationship between structure and activity is explored.

Entities:  

Mesh:

Substances:

Year:  2005        PMID: 16261252     DOI: 10.1007/s00018-005-5373-z

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN: 1420-682X            Impact factor:   9.261


  136 in total

1.  Positive selection drives lactoferrin evolution in mammals.

Authors:  Guo Ming Liang; Xun Ping Jiang
Journal:  Genetica       Date:  2010-04-18       Impact factor: 1.082

Review 2.  Studies on anticancer activities of antimicrobial peptides.

Authors:  David W Hoskin; Ayyalusamy Ramamoorthy
Journal:  Biochim Biophys Acta       Date:  2007-11-22

Review 3.  A current review of molecular mechanisms regarding osteoarthritis and pain.

Authors:  Andrew S Lee; Michael B Ellman; Dongyao Yan; Jeffrey S Kroin; Brian J Cole; Andre J van Wijnen; Hee-Jeong Im
Journal:  Gene       Date:  2013-07-02       Impact factor: 3.688

4.  A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency.

Authors:  Falk Duchardt; Ivo R Ruttekolk; Wouter P R Verdurmen; Hugues Lortat-Jacob; Jochen Bürck; Hansjörg Hufnagel; Rainer Fischer; Maaike van den Heuvel; Dennis W P M Löwik; Geerten W Vuister; Anne Ulrich; Michel de Waard; Roland Brock
Journal:  J Biol Chem       Date:  2009-10-26       Impact factor: 5.157

Review 5.  Antimicrobial peptide resistance in Neisseria meningitidis.

Authors:  Yih-Ling Tzeng; David S Stephens
Journal:  Biochim Biophys Acta       Date:  2015-05-19

Review 6.  Antimicrobial peptides with cell-penetrating peptide properties and vice versa.

Authors:  Katrin Splith; Ines Neundorf
Journal:  Eur Biophys J       Date:  2011-02-19       Impact factor: 1.733

7.  Design and high-level expression of a hybrid antimicrobial peptide LF15-CA8 in Escherichia coli.

Authors:  Xing-Jun Feng; Li-Wei Xing; Di Liu; Xue-Ying Song; Chun-Long Liu; Jing Li; Wen-Shan Xu; Zhong-Qiu Li
Journal:  J Ind Microbiol Biotechnol       Date:  2013-11-27       Impact factor: 3.346

8.  A role for antimicrobial peptides in intestinal microsporidiosis.

Authors:  G J Leitch; C Ceballos
Journal:  Parasitology       Date:  2008-12-12       Impact factor: 3.234

Review 9.  Lactoferrin as a natural immune modulator.

Authors:  Jeffrey K Actor; Shen-An Hwang; Marian L Kruzel
Journal:  Curr Pharm Des       Date:  2009       Impact factor: 3.116

Review 10.  Vibrio Iron Transport: Evolutionary Adaptation to Life in Multiple Environments.

Authors:  Shelley M Payne; Alexandra R Mey; Elizabeth E Wyckoff
Journal:  Microbiol Mol Biol Rev       Date:  2015-12-09       Impact factor: 11.056

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.