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Insufficient research on the material basis and functional product development of horse bones has led to the waste of resources. This paper, as the by-product of horse meat bone marrow was the object, aimed to discover the flavor and antioxidant activity of novel collagen peptides. Two peptides, HBMP-1-1 and HBMP-2-1, were isolated and purified from horse bone marrow collagen protein (HBMP) hydrolysates. The combination of spectroscopic and chromatographic methods including SDS-PAGE, UV, FT-IR, CD, and SEM identified the structures of the peptides. The amino acid composition, flavor characteristics, and antioxidant activity were also evaluated. SDS-PAGE analysis showed that the molecular weight of the two peptides was concentrated under 4.1 kDa. The total amino acid contents of the HBMP-1-1 was up to 570.779 mg/g. Leucine, alanine, and glutamicacid were the predominant amino acids in HBMP-1-1 with high nutritional value, and it contained 10.07% β-folding, 46.39% β-turn, and 43.54% random coil structure. The peptide sequences IDDPTDSKPE, LNGKLTGM, ELDEGYVPK, AFQEDPDKF, and FVGKVVDPTQK with molecular weights of 1116.51, 833.45, 1049.51, 1096.49, and 1217.69 Da were detected using LC-MS/MS. The results of the antioxidant activity test showed that separation and purification significantly improved the bioactivity of the protein. The half-inhibition rate of HBMP-1-1 against DPPH, ABTS, and hydroxyl radicals were 0.054, 0.050, and 0.137 mg/mL, respectively. This article provides a scientific basis for clarifying the material basis of horse bone marrow collagen peptides. Also, it provides new approaches and ideas for exploring efficient and safe bone-derived lead compounds and products. [ABSTRACT FROM AUTHOR]

The construction of peptides to mimic heterogeneous proteins such as type I collagen plays a pivotal role in deciphering their function and pathogenesis. However, progress in the field has been severely hampered by the lack of capability to create stable heterotrimers with desired functional sequences and without the effect of homotrimers. We have herein developed a set of triblock peptides that can assemble into collagen mimetic heterotrimers with desired amino acids and are free from the interference of homotrimers. The triblock peptides comprise a central collagen-like block and two oppositely charged N-/C-terminal blocks, which display inherent incompetency of homotrimer formation. The favorable electrostatic attraction between two paired triblock peptides with complementary terminal charged sequences promptly leads to stable heterotrimers with controlled chain composition. The independence of the collagen-like block from the two terminal blocks endows this system with the adaptability to incorporate desired amino acid sequences while maintaining the heterotrimer structure. The triblock peptides provide a versatile and robust tool to mimic the composition and function of heterotrimer collagen and may have great potential in the design of innovative peptides mimicking heterogeneous proteins. [ABSTRACT FROM AUTHOR]

Synthesis of long peptides is generally considered as a challenge to peptide chemists, in addition to producing significant amounts of toxic waste, such as DMF. Here we show that using solvent‐less methods, such as ball milling, enabled the production of the hexapeptide Boc‐(Ala‐Phe‐Gly)2‐OBn at the gram scale with high overall yield (77 %, 5 linear steps). This is the longest peptide chain synthesized in a ball mill to date, in which the amino acid sequence is precisely controlled. This study complements the current fundamental knowledge required to synthesize longer and more difficult peptide chains (or small proteins) by using peptide fragment couplings in a ball mill. [ABSTRACT FROM AUTHOR]