Mechanism of promoted dipeptide formation on hydroxyapatite crystal surfaces

Wu, Jia; Zhang, ZhiShen; Yu, Xinwei; Pan, Haihua; Jiang, Wenge; Xu, Xurong; Tang, Ruikang

doi:10.1007/s11434-010-4314-x

Cited by 10 publications

(5 citation statements)

References 40 publications

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“…The activation energy of the formation of DKP from Ala 2 is found to be lower when compared to the formation of Ala 2 from the condensation of two alanine molecules [ 55 ]. The high temperature favoring the formation of DKP in this study is in accord with the following studies [ 39 , 42 , 44 , 56 ]. Under hydrothermal conditions, kinetic analysis of dimer formation and DKPs was also reported by Kawamura and co-workers [ 57 , 58 ].…”

Section: Resultssupporting

confidence: 92%

Thermal Condensation of Glycine and Alanine on Metal Ferrite Surface: Primitive Peptide Bond Formation Scenario

Iqubal

Sharma

Jheeta³

et al. 2017

Life

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The amino acid condensation reaction on a heterogeneous mineral surface has been regarded as one of the important pathways for peptide bond formation. Keeping this in view, we have studied the oligomerization of the simple amino acids, glycine and alanine, on nickel ferrite (NiFe2O4), cobalt ferrite (CoFe2O4), copper ferrite (CuFe2O4), zinc ferrite (ZnFe2O4), and manganese ferrite (MnFe2O4) nanoparticles surfaces, in the temperature range from 50–120 °C for 1–35 days, without applying any wetting/drying cycles. Among the metal ferrites tested for their catalytic activity, NiFe2O4 produced the highest yield of products by oligomerizing glycine to the trimer level and alanine to the dimer level, whereas MnFe2O4 was the least efficient catalyst, producing the lowest yield of products, as well as shorter oligomers of amino acids under the same set of experimental conditions. It produced primarily diketopiperazine (Ala) with a trace amount of alanine dimer from alanine condensation, while glycine was oligomerized to the dimer level. The trend in product formation is in accordance with the surface area of the minerals used. A temperature as low as 50 °C can even favor peptide bond formation in the present study, which is important in the sense that the condensation process is highly feasible without any sort of localized heat that may originate from volcanoes or hydrothermal vents. However, at a high temperature of 120 °C, anhydrides of glycine and alanine formation are favored, while the optimum temperature for the highest yield of product formation was found to be 90 °C.

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Section: Resultssupporting

confidence: 92%

Thermal Condensation of Glycine and Alanine on Metal Ferrite Surface: Primitive Peptide Bond Formation Scenario

Iqubal

Sharma

Jheeta³

et al. 2017

Life

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“…The catalytic formation of dipeptides was investigated for l - Asp-NPs and l - Pro-NPs as well as NPs carrying the equimolar mixture of different amino acids, with the corresponding CD spectra shown in Figure S14. Considering the spectrum of conditions that were used in the past, with reaction times of up to several tens of days and heating with temperatures as high as 100, 130, and even 190 °C, − the conditions used herein are mild, and the duration of the reaction is short.…”

Section: Results and Discussionmentioning

confidence: 99%

Chiral Ceramic Nanoparticles and Peptide Catalysis

et al. 2017

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The chirality of nanoparticles (NPs) and their assemblies has been investigated predominantly for noble metals and II-VI semiconductors. However, ceramic NPs represent the majority of nanoscale materials in nature. The robustness and other innate properties of ceramics offer technological opportunities in catalysis, biomedical sciences, and optics. Here we report the preparation of chiral ceramic NPs, as represented by tungsten oxide hydrate, WO·HO, dispersed in ethanol. The chirality of the metal oxide core, with an average size of ca. 1.6 nm, is imparted by proline (Pro) and aspartic acid (Asp) ligands via bio-to-nano chirality transfer. The amino acids are attached to the NP surface through C-O-W linkages formed from dissociated carboxyl groups and through amino groups weakly coordinated to the NP surface. Surprisingly, the dominant circular dichroism bands for NPs coated by Pro and Asp are different despite the similarity in the geometry of the NPs; they are positioned at 400-700 nm and 500-1100 nm for Pro- and Asp-modified NPs, respectively. The differences in the spectral positions of the main chiroptical band for the two types of NPs are associated with the molecular binding of the two amino acids to the NP surface; Asp has one additional C-O-W linkage compared to Pro, resulting in stronger distortion of the inorganic crystal lattice and greater intensity of CD bands associated with the chirality of the inorganic core. The chirality of WO·HO atomic structure is confirmed by atomistic molecular dynamics simulations. The proximity of the amino acids to the mineral surface is associated with the catalytic abilities of WO·HO NPs. We found that NPs facilitate formation of peptide bonds, leading to Asp-Asp and Asp-Pro dipeptides. The chiroptical activity, chemical reactivity, and biocompatibility of tungsten oxide create a unique combination of properties relevant to chiral optics, chemical technologies, and biomedicine.

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“…water and methanol added explicitly in the neighborhood of glycine), the hydroxyapatite reduced the activation barrier for the formation of dipeptides by more than 50%. The presence of this mineral compound or similar catalyst decreased the distance between amino and carboxyl groups on neighboring molecules and extends the contact time of the reaction group [ 38 ].…”

Section: Discussionmentioning

confidence: 99%

Assisted dipeptide bond formation: glycine as a case study

Achour

Hosni

Darghouthi

et al. 2021

Heliyon

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Peptide bond formation is a crucial chemical process that dominates most biological mechanisms and is claimed to be a governing factor in the origin of life. Dipeptides made from glycine are studied computationally via Density Functional Theory (DFT) using two different basis sets. This reaction was investigated from both a thermodynamic and kinetic point of view. The effect of explicit assistance via the introduction of discrete solvent molecules was investigated. Water, methanol, and cyclohexane were all employed as solvent media in addition to gas to investigate their effects on the mechanism of peptide bond formation. This computational investigation revealed that methanol is slightly better than water to leverage peptide bond formation both kinetically and thermodynamically, while cyclohexane, a non-polar and non-protic solvent, is the least effective after gas as a medium of solvation. Energetic results in the gas environment are very close to those obtained in polar and protic solvents, suggesting that peptide bonds can be formed under interstellar conditions.

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Mechanism of promoted dipeptide formation on hydroxyapatite crystal surfaces

Cited by 10 publications

References 40 publications

Thermal Condensation of Glycine and Alanine on Metal Ferrite Surface: Primitive Peptide Bond Formation Scenario

Thermal Condensation of Glycine and Alanine on Metal Ferrite Surface: Primitive Peptide Bond Formation Scenario

Chiral Ceramic Nanoparticles and Peptide Catalysis

Assisted dipeptide bond formation: glycine as a case study

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