Self-Assembling Synthetic Oligopeptide-Based Gelators

Synthetic self-assembling oligopeptide gelators are an important class of compounds which form thermoreversible gels in various organic solvents as well as in aqueous medium. These gels are soft, viscoelastic materials which are envisaged for useful applications in biological and material sciences. The terminally protected self-assembling synthetic tripeptide Boc-Ala-Aib-β-Ala-OMe 1 (Aib: α-aminoisobutyric acid i.e. dimethyl glycine and β-Ala: β-Alanine) forms gels in various organic solvents, whereas its structural analog i.e. the peptide Boc-Ala-Gly-β-Ala-OMe 2 (another self-assembling synthetic tripeptide) fails to form gels under similar conditions and this issue has been addressed. The terminally protected tripeptide Boc-Ala-Val-Ala-OMe 3 has been found to form gels in different aromatic organic solvents. Several structural analogs of peptide 3 [using small structural changes either in protecting groups (at the N or C-terminal position) or in amino acid side chains] have been synthesized, characterized and studied for gelation to address the question how structural changes can regulate the gelation property. Results of the gelation studies indicate that some structural changes are useful to make new peptide gelators with some variations in gelation property and efficiency, while a few structural changes in the protecting groups are really detrimental, leading to abolition the gelation property. These gels are studied by scanning electron microscopy (SEM), transmission electron microscopy (TEM), Fourier-Transform Infrared (FT-IR) spectroscopy and ¹H NMR studies.     

Microwave-assisted extraction (MAE) combined with gas chromatography–mass spectrometry (GC–MS) for determination of volatile small molecules to evaluate compatibility of antimicrobial peptide PL-5 spray with packaging materials

A simple and efficient method involving microwave-assisted extraction (MAE) combined with GC–MS was established to determine 1,3-di-tert-butylbenzene (DBB), 2,4-di-tert-butylphenol (DBP), 3,5-di-tert-butyl-4-hydroxybenzaldehyde (DBHBA) for evaluating the compatibility of antimicrobial peptide PL-5 spray with drug-packaging materials. In this study, the antimicrobial peptide PL-5 spray was purified using a Welchrom C18 column, and the high-density polyethylene spray bottle with liquid collection tube was first mixed with absolute ethanol, which would be subjected to MAE for further measurement by GC–MS. Various experimental parameters were systematically optimized, and good linearities were obtained within the range of 0.05–1.00 μg/mL for DBB and DBHBA and 0.50–10.00 μg/mL for DBP, with limits of detection (LODs) of 0.99 ng/mL (DBB), 16.34 ng/mL (DBP), and 1.64 ng/mL (DBHBA). Satisfactory recoveries that ranged from 96.0% to 107.2% were acquired, and the relative standard deviation was ≤ 4.7%. The results showed that the maximum daily usage of DBB, DBP, and DBHBA was 9.859, 163.445, and 16.399 ng, respectively, which was far below the corresponding permitted daily exposure values according to the safety assessment, indicating that the migration of analytes did not bring any potential safety risk. The compatibility between the drug and the packaging materials was favorable.     

含酪氨酸和色氨酸的肽内电子转移的溶剂重组能计算

基于连续介质模型，本文考察了多肽体系Trp-(Pro)n-Tyr (n=1,2) 从酪氨酸到色氨酸的分子内电子转移，并根据电荷定域的反应物和产物构型和线性反应坐标近似构造了电子转移的双势阱，通过势能曲线的交叉点确定了电子转移过渡态。本文重点讨论了电子转移溶剂重组能。根据作者的非平衡溶剂化理论和可极化连续介质模型编写了溶剂重组能计算程序并用于本文体系的计算。计算得到Trp-Pro-Tyr 和Trp-(Pro)2-Tyr.体系的溶剂重组能分别为20.89 kcal/mol和25.30 kcal/mol.     

A Micro-Scale Model to Monitor the Major Proteins in Human Urine Before and After Medication with Angiotensin-Converting Enzyme Inhibitor: A Preliminary Study

A simple and micro-scale liquid chromatographic (LC) method coupled with mass spectrometry was developed for analyzing major proteins in human urine. After one-step sample preparation, proteins were precipitated, redissolved, and digested. Only micro-liter level (10 μL) of urine was sufficient for major protein identification. This method was applied in clinical study, and urine proteins were monitored after medication with angiotensin-converting enzyme inhibitor within 24 hr. This method can identify many important proteins in human urine. Bioactive peptides associated with blood pressure control can also be identified simultaneously. We hope this simple method may prove useful in clinical research and disease diagnosis.     

Learning from Peptides to Access Functional Precision Polymer Sequences

Functional precision polymers based on monodisperse oligo(N‐substituted acrylamide)s and oligo(2‐substituted‐α‐hydroxy acid)s have been synthesized. The discrete sequences originate from a direct translation of side‐chain functionality sequences of a peptide with well‐studied properties. The peptide was previously selected to solubilize the photosensitizer meta‐tetra(hydroxyphenyl)chlorin. The resulting peptidomimetic formulation additives preserve the drug solubilization and release characteristics of the parent peptide. In some cases, superior properties are obtained, reaching up to 40 % higher payloads and 27‐times faster initial drug release.