Specificity of Lipoprotein Chaperones for the Characteristic Lipidated Structural Motifs of their Cognate Lipoproteins

Lipoprotein‐binding chaperones mediate intracellular transport of lipidated proteins and determine their proper localisation and functioning. Understanding of the exact structural parameters that determine recognition and transport by different chaperones is of major interest. We have synthesised several lipid‐modified peptides, representative of different lipoprotein classes, and have investigated their binding to the relevant chaperones PDEδ, UNC119a, UNC119b, and galectins‐1 and ‐3. Our results demonstrate that PDEδ recognises S‐isoprenylated C‐terminal peptidic structures but not N‐myristoylated peptides. In contrast, UNC119 proteins bind only mono‐N‐myristoylated, but do not recognise doubly lipidated and S‐isoprenylated peptides at the C terminus. For galectins‐1 and ‐3, neither binding to N‐acylated, nor to C‐terminally prenylated peptides could be determined. These results shed light on the specificity of the chaperone‐mediated cellular lipoprotein transport systems.     

Bioactive peptides with antidiabetic properties: a review

Diabetes mellitus is a complex disorder characterised by insufficient insulin production or insulin resistance. Disease incidence is accumulating at a rapidly increasing rate, resulting in a considerable social, health and economic burden in the modern world. Bioactive peptides show significant potential for use in health management strategies, particularly as components of drugs and functional foods for diabetes treatment. Many antidiabetic bioactive peptides have been isolated and validated. The aim of this review was to update the state of knowledge of the origin, structural characteristics and action. Additionally, the potential mechanisms of bioactive peptides on key enzymes and proteins, such as α-amylase, α-glucosidase, glucagon-like peptides and dipeptidyl peptidase-IV, that participate in glycaemic level control from the intake of carbohydrates to blood glucose regulation were overviewed. This knowledge should facilitate research and industrial efforts to better understand and evaluate the potential of bioactive peptides with antidiabetic properties for blood glucose level management.     

Valorisation of protein hydrolysates from animal by-products: perspectives on bitter taste and debittering methods: a review

Conversion of animal by-products to high value-added food ingredients is one of the top trends in the slaughter industry. Enzymatic hydrolysis of animal by-products can generate protein hydrolysates, which provides an opportunity for effective utilisation. However, bitterness of protein hydrolysate is a major undesirable aspect for various applications. In this review, the current knowledge on protein hydrolysates from animal by-products is briefly reviewed. The structural features of bitter peptides and bitter taste receptors are summarised. Moreover, the potential approaches for debittering protein hydrolysates are highlighted, including exopeptidase treatment, Maillard reaction, plastein reaction and encapsulation. In addition, the current debittering strategies and challenges are also discussed. This article presents some opportunities to utilise protein hydrolysates from animal by-products and their debittering methods.     

An Overview,Advantages and Therapeutic Potential of Nonpeptide Positive Allosteric Modulators of Glucagon-Like Peptide-1 Receptor

Due to uncomfortable injection regimens of peptidic agonists of glucagon-like peptide-1 receptor (GLP-1R), orally available nonpeptide positive allosteric modulators (PAMs) of GLP-1Rs are foreseen as the possible future mainstream therapy for type 2 diabetes. Herein, current GLP-1R PAMs are reviewed. Based on the effectiveness and in silico predicted physicochemical properties, pharmacokinetics, and toxicity, possible candidates for further development as oral drugs were selected. The suggestion is that GLP-1R PAMs might be used orally alone or in combination with dipeptidyl peptidase-4 (DPP-4) inhibitors, which could offer an optimal treatment option next to metformin monotherapy in type 2 diabetes mellitus, or in a wider spectrum of indications. Quercetin acts as a GLP-1R PAM and DPP-4 inhibitor, and therefore, might be considered as a pioneering agent with a dual mechanism of action, in terms of GLP-1R positive allosteric modulation and DPP-4 inhibition for potentiating GLP-1 dependent effects.     

Modular Self‐Assembling Peptide Platform with a Tunable Thermoresponsiveness via a Single Amino Acid Substitution

The introduction of a stimulus‐responsive property is an effective way to increase the applicability of functional materials in the field of nanobiotechnology. Herein, a peptide platform is devised for constructing elastin‐like peptide amphiphiles (ELPAs) that exhibit a temperature‐responsiveness that can be easily tuned via a single N‐terminal amino acid substitution at the final step of peptide synthesis. Due to the modular property of peptides, the platform based on a miniaturized elastin‐like peptide (MELP) can be conjugated with various bioactive peptide sequences in diverse macromolecular topologies. First, the MELP platform is coupled with a short linear RGD peptide. The ELPAs of the peptide conjugates exhibit rapid aggregation (coacervation) and retard disaggregation in response to heating and cooling, respectively. Second, the platform is grafted with an α‐helical guest peptide in a lariat‐type structure, which forms ELPAs that undergo faster disassembly than the ELPAs without the guest peptide in response to temperature increases. Interestingly, the critical temperatures for the thermoresponsive behaviors are commonly dependent on the hydrophobic and aromatic properties of the N‐terminal amino acid residues. These results suggest that this peptide platform possesses great potential for use in the development of smart materials in wide‐ranging applications related to temperature change.     

Phototemtide A,a Cyclic Lipopeptide Heterologously Expressed from Photorhabdus temperata Meg1, Shows Selective Antiprotozoal Activity

A new cyclic lipopeptide, phototemtide A ( 1 ), was isolated from Escherichia coli expressing the biosynthetic gene cluster pttABC from Photorhabdus temperata Meg1. The structure of 1 was elucidated by HR-ESI-MS and NMR experiments. The absolute configurations of amino acids and 3-hydroxyoctanoic acid in 1 were determined by using the advanced Marfey's method and comparison after total synthesis of 1 , respectively. Additionally, three new minor derivatives, phototemtides B–D ( 2 – 4 ), were identified by detailed HPLC–MS analysis. Phototemtide A ( 1 ) showed weak antiprotozoal activity against Plasmodium falciparum, with an IC₅₀ value of 9.8 μm . The biosynthesis of phototemtides A–D ( 1 – 4 ) was also proposed.     

Hydrolytic degree and antioxidant activity of purified casein characterised by different haplotypes (αs1-, β- and k-casein) after enzymatic hydrolysis with pepsin and enzymatic extract from Pleurotus eryngii

The aim of this study was to estimate the hydrolytic degree and antioxidant activity of purified casein characterised by different haplotypes (α_s1-, β- and k-casein) after in vitro digestion with two different enzymatic systems: pepsin from porcine gastric mucosa (EP) and a crude enzymatic extract from the edible mushroom Pleurotus eryngii. The used enzymes showed a different mode of casein catalysis with a consequent production of peptides of different antioxidant activity. The CN haplotype significantly influenced peptides production; in fact, the amino acid substitutions caused by genetic polymorphisms at the α_s1-, β- and k-CN loci influenced the sites of enzymatic cleavage and therefore the produced peptides. The above is evidenced by the different antioxidant activity found in the hydrolysates depending on the used enzymatic system, the CN haplotype, and the CN haplotype × enzymatic treatment interaction. The findings of this study are a perspective for the production of specific foods that exert a biological effect in addition to the nutritional one.     

不同长度金属结合肽对大肠杆菌吸附钯性能的影响

利用微生物吸附法回收铂族金属(PGMs)有较大的应用前景，然而利用基因工程手段改造微生物胞外金属结合基团，进而提升微生物的吸附量与特异性仍是一项挑战。本研究利用微生物表面展示技术，在大肠杆菌(Escherichia coli，简写为E. coli)BL21菌株外膜上展示了不同长度的金属结合肽(EC10、EC20、EC30)，并解析了其对钯(Pd(II))的吸附行为。结果表明，在E.coli BL21表面展示不同长度金属结合肽均能增强其对Pd(II)的吸附量。其中，表面展示了EC20的菌株(简写为E. coli EC20)吸附量最高，为144.25 mg/g，是未进行表面展示菌株的1.14倍；E. coli BL21和E. coli EC20均能够从含多种金属离子的工业废水中选择性吸附Pd(II)和Pt(IV)，两株菌对Pd(II)吸附率分别为96.2%和99.0%。以上研究表明利用表面展示技术增加微生物外膜金属结合基团是一种有效提升微生物吸附能力的手段。