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Multifunctional iron bound lactoferrin and nanomedicinal approaches to enhance its bioactive functions

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Version 2 2024-06-06, 06:45
Version 1 2015-08-18, 15:33
journal contribution
posted on 2024-06-06, 06:45 authored by JR Kanwar, K Roy, Y Patel, S-F Zhou, MR Singh, D Singh, M Nasir, R Sehgal, A Sehgal, RS Singh, S Garg, RK Kanwar
Lactoferrin (Lf), an iron-binding protein from the transferrin family has been reported to have numerous functions. Even though Lf was first isolated from milk, it is also found in most exocrine secretions and in the secondary granules of neutrophils. Antimicrobial and anti-inflammatory activity reports on lactoferrin identified its significance in host defense against infection and extreme inflammation. Anticarcinogenic reports on lactoferrin make this protein even more valuable. This review is focused on the structural configuration of iron-containing and iron-free forms of lactoferrin obtained from different sources such as goat, camel and bovine. Apart for emphasizing on the specific beneficial properties of lactoferrin from each of these sources, the general antimicrobial, immunomodulatory and anticancer activities of lactoferrin are discussed here. Implementation of nanomedicinial strategies that enhance the bioactive function of lactoferrin are also discussed, along with information on lactoferrin in clinical trials.

History

Journal

Molecules

Volume

20

Pagination

9703-9731

Location

Basel, Switzerland

Open access

  • Yes

eISSN

1420-3049

Language

eng

Publication classification

C Journal article, C1.1 Refereed article in a scholarly journal

Copyright notice

2015, The Authors

Issue

6

Publisher

MDPI