[HTML][HTML] Diverse mechanisms of antimicrobial activities of lactoferrins, lactoferricins, and other lactoferrin-derived peptides

Š Gruden, N Poklar Ulrih - International journal of molecular sciences, 2021 - mdpi.com
Lactoferrins are an iron-binding glycoprotein that have important protective roles in the
mammalian body through their numerous functions, which include antimicrobial, antitumor …

[HTML][HTML] Candida Infections and Therapeutic Strategies: Mechanisms of Action for Traditional and Alternative Agents

GC de Oliveira Santos, CC Vasconcelos… - Frontiers in …, 2018 - frontiersin.org
The Candida genus comprises opportunistic fungi that can become pathogenic when the
immune system of the host fails. Candida albicans is the most important and prevalent …

[HTML][HTML] Lactoferrin's anti-cancer properties: Safety, selectivity, and wide range of action

A Cutone, L Rosa, G Ianiro, MS Lepanto… - Biomolecules, 2020 - mdpi.com
Despite recent advances in cancer therapy, current treatments, including radiotherapy,
chemotherapy, and immunotherapy, although beneficial, present attendant side effects and …

The cation− π interaction

JC Ma, DA Dougherty - Chemical reviews, 1997 - ACS Publications
Noncovalent interactions play a dominant role in many forefront areas of modern chemistry,
from materials design to molecular biology. A detailed understanding of the physical origin …

Lactoferrin a multiple bioactive protein: an overview

IA García-Montoya, TS Cendón… - … et Biophysica Acta (BBA …, 2012 - Elsevier
BACKGROUND: Lactoferrin (Lf) is an 80kDa iron-binding glycoprotein of the transferrin
family. It is abundant in milk and in most biological fluids and is a cell-secreted molecule that …

[HTML][HTML] Lactoferrin in aseptic and septic inflammation

MS Lepanto, L Rosa, R Paesano, P Valenti, A Cutone - Molecules, 2019 - mdpi.com
Lactoferrin (Lf), a cationic glycoprotein able to chelate two ferric irons per molecule, is
synthesized by exocrine glands and neutrophils. Since the first anti-microbial function …

Lactoferrin: Molecular structure, binding properties and dynamics of lactoferrin

EN Baker, HM Baker - Cellular and Molecular Life Sciences, 2005 - Springer
Lactoferrin (Lf), a prominent protein in milk, many other secretory fluids and white blood
cells, is a monomeric, 80-kDa glycoprotein, with a single polypeptide chain of about 690 …

Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution

SA Moore, BF Anderson, CR Groom, M Haridas… - Journal of molecular …, 1997 - Elsevier
The three-dimensional structure of diferric bovine lactoferrin (bLf) has been determined by X-
ray crystallography in order to investigate the factors that influence iron binding and release …

Remarks about protein structure precision

DWJ Cruickshank - Acta Crystallographica Section D: Biological …, 1999 - journals.iucr.org
Full-matrix least squares is taken as the basis for an examination of protein structure
precision. A two-atom protein model is used to compare the precisions of unrestrained and …

Occurrence, structure, biochemical properties and technological characteristics of lactoferrin

JM Steijns, ACM Van Hooijdonk - British Journal of Nutrition, 2000 - cambridge.org
The structure of the iron-binding glycoprotein lactoferrin, present in milk and other exocrine
secretions, has been elucidated in great detail, both the three-dimensional protein structure …