Unknown

Dataset Information

0

Antimicrobial lactoferrin peptides: the hidden players in the protective function of a multifunctional protein.


ABSTRACT: Lactoferrin is a multifunctional, iron-binding glycoprotein which displays a wide array of modes of action to execute its primary antimicrobial function. It contains various antimicrobial peptides which are released upon its hydrolysis by proteases. These peptides display a similarity with the antimicrobial cationic peptides found in nature. In the current scenario of increasing resistance to antibiotics, there is a need for the discovery of novel antimicrobial drugs. In this context, the structural and functional perspectives on some of the antimicrobial peptides found in N-lobe of lactoferrin have been reviewed. This paper provides the comparison of lactoferrin peptides with other antimicrobial peptides found in nature as well as interspecies comparison of the structural properties of these peptides within the native lactoferrin.

SUBMITTER: Sinha M 

PROVIDER: S-EPMC3608178 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

altmetric image

Publications

Antimicrobial lactoferrin peptides: the hidden players in the protective function of a multifunctional protein.

Sinha Mau M   Kaushik Sanket S   Kaur Punit P   Sharma Sujata S   Singh Tej P TP  

International journal of peptides 20130213


Lactoferrin is a multifunctional, iron-binding glycoprotein which displays a wide array of modes of action to execute its primary antimicrobial function. It contains various antimicrobial peptides which are released upon its hydrolysis by proteases. These peptides display a similarity with the antimicrobial cationic peptides found in nature. In the current scenario of increasing resistance to antibiotics, there is a need for the discovery of novel antimicrobial drugs. In this context, the struct  ...[more]

Similar Datasets

| S-EPMC9965131 | biostudies-literature
| S-EPMC11846078 | biostudies-literature
2018-09-15 | GSE113347 | GEO
| S-EPMC10862732 | biostudies-literature
| S-EPMC7464209 | biostudies-literature
| S-EPMC525416 | biostudies-literature