Identification of mineral-binding peptides that discriminate between chalcopyrite and enargite

2016 ◽  
Vol 114 (5) ◽  
pp. 998-1005 ◽  
Author(s):  
Susan Curtis ◽  
Franziska L. Lederer ◽  
W. Scott Dunbar ◽  
Ross T.A. MacGillivray
Foods ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 1402
Author(s):  
Xiaohong Sun ◽  
Roghayeh Amini Sarteshnizi ◽  
Ruth T. Boachie ◽  
Ogadimma D. Okagu ◽  
Raliat O. Abioye ◽  
...  

Iron, zinc, and calcium are essential micronutrients that play vital biological roles to maintain human health. Thus, their deficiencies are a public health concern worldwide. Mitigation of these deficiencies involves micronutrient fortification of staple foods, a strategy that can alter the physical and sensory properties of foods. Peptide–mineral complexes have been identified as promising alternatives for mineral-fortified functional foods or mineral supplements. This review outlines some of the methods used in the determination of the mineral chelating activities of food protein-derived peptides and the approaches for the preparation, purification and identification of mineral-binding peptides. The structure–activity relationship of mineral-binding peptides and the potential use of peptide–mineral complexes as functional food ingredients to mitigate micronutrient deficiency are discussed in relation to their chemical interactions, solubility, gastrointestinal digestion, absorption, and bioavailability. Finally, insights on the current challenges and future research directions in this area are provided.


2017 ◽  
Vol 5 (4) ◽  
pp. 663-668
Author(s):  
Jae Sung Lee ◽  
Xiaohua Yu ◽  
Amy J. Wagoner Johnson ◽  
William L. Murphy

Modular growth factor peptides that bind to calcium phosphate minerals via an osteocalcin-inspired sequence show significantly enhanced binding stability in serum.


Blood ◽  
2004 ◽  
Vol 103 (4) ◽  
pp. 1356-1363 ◽  
Author(s):  
Barbara P. Schick ◽  
David Maslow ◽  
Adrianna Moshinski ◽  
James D. San Antonio

Abstract Patients given unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH) for prophylaxis or treatment of thrombosis sometimes suffer serious bleeding. We showed previously that peptides containing 3 or more tandem repeats of heparin-binding consensus sequences have high affinity for LMWH and neutralize LMWH (enoxaparin) in vivo in rats and in vitro in citrate. We have now modified the (ARKKAAKA)n tandem repeat peptides by cyclization or by inclusion of hydrophobic tails or cysteines to promote multimerization. These peptides exhibit high-affinity binding to LMWH (dissociation constant [Kd], ≈ 50 nM), similar potencies in neutralizing anti–Factor Xa activity of UFH and enoxaparin added to normal plasma in vitro, and efficacy equivalent to or greater than protamine. Peptide (ARKKAAKA)3VLVLVLVL was most effective in all plasmas from enoxaparin-treated patients, and was 4- to 20-fold more effective than protamine. Several other peptide structures were effective in some patients' plasmas. All high-affinity peptides reversed inhibition of thrombin-induced clot formation by UFH. These peptides (1 mg/300 g rat) neutralized 1 U/mL anti–Factor Xa activity of enoxaparin in rats within 1 to 2 minutes. Direct blood pressure and heart rate measurements showed little or no hemodynamic effect. These heparin-binding peptides, singly or in combination, are potential candidates for clinical reversal of UFH and LMWH in humans.


2021 ◽  
Author(s):  
Makoto Ozaki ◽  
Shuhei Yoshida ◽  
Takaaki Tsuruoka ◽  
Kenji Usui

Our method can produce uniquely shaped gold nanostructures in lower HAuCl4 concentration than conventional methods by intracellular functions using peptide assembled structures as a template.


2019 ◽  
Vol 124 (1) ◽  
pp. 61-68 ◽  
Author(s):  
Xingqing Xiao ◽  
Zhifeng Kuang ◽  
B. J. Burke ◽  
Yaroslav Chushak ◽  
Barry L. Farmer ◽  
...  

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