- A dynamic combinatorial library for biomimetic recognition of dipeptides in water
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Small peptides are involved in countless biological processes. Hence selective binding motifs for peptides can be powerful tools for labeling or inhibition. Finding those binding motifs, especially in water which competes for intermolecular H-bonds, poses an enormous challenge. A dynamic combinatorial library can be a powerful method to overcome this issue. We previously reported artificial receptors emerging form a dynamic combinatorial library of peptide building blocks. In this study we aimed to broaden this scope towards recognition of small peptides. Employing CXC peptide building blocks, we found that cyclic dimers of oxidized CFC bind to the aromatic peptides FF and YY (K ≈ 229-702 M-1), while AA binds significantly weaker (K ≈ 65-71 M-1).
- Klepel, Florian,Ravoo, Bart Jan
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- Dietary Dityrosine Induces Mitochondrial Dysfunction by Diminished Thyroid Hormone Function in Mouse Myocardia
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Oxidized tyrosine products (OTP) have been detected in commercial foods with high protein content, such as meat and milk products. OTP intake induces tissue oxidative stress and affects the normal activity of the hypothalamic-pituitary-thyroid axis (HPT). This study aims to investigate the effects of OTP and their main product, dityrosine (Dityr), on mouse myocardial function and myocardial energy metabolism. Mice received daily intragastric administration of either tyrosine (Tyr; 420 μg/kg body weight), Dityr (420 μg/kg body weight), or OTP (1909 μg/kg body weight) for 35 days. Additionally, H9c2 cells were incubated with various concentrations of Dityr for 72 h. We found that OTP and pure Dityr induced oxidative stress in growing mice and in H9c2 cells, resulting in a redox state imbalance, myocardial injury, mitochondrial dysfunction, and energy metabolism disorder. Dityr interferes with T3 regulation of the myocardium via the PI3K/AKT/GSK3β pathway, leading to myocardial mitochondrial damage and energy metabolism disorders. Food-borne OTP, especially Dityr, can disrupt thyroid hormone function in mouse myocardia leading to mitochondrial dysfunction, energy metabolism disorder, and oxidative stress.
- Ge, Yueting,Li, Bowen,Lu, Yipin,Ma, Shuhua,Ren, Haoyi,Tang, Xue,Xu, Ying,Yang, Shaojun,Zhang, Kai,Zhao, Qi
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- Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins
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A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the l- and d-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach.
- Usuki, Hirokazu,Yamamoto, Yukihiro,Arima, Jiro,Iwabuchi, Masaki,Miyoshi, Shozo,Nitoda, Teruhiko,Hatanaka, Tadashi
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supporting information; experimental part
p. 2327 - 2335
(2011/05/02)
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- Compositions and Methods for Binding Lysophosphatidic Acid
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Compositions and methods for making and using anti-LPA agents, for example, monoclonal antibodies, are described.
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