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The growing concern over antimicrobial resistance in Cutibacterium acnes ( C. acnes ) has spurred interest in alternative acne treatments, particularly herbal medicines. This study evaluates the binding affinities of established anti-acne agents—ketoconazole (KET) and tetracycline (TET)—alongside natural compounds, brazilin (BRA) and hematein (HEM), derived from Caesalpinia sappan L. ( C. sappan ), to C. acnes lipase. Through molecular docking and dynamics simulations, we demonstrate that the asymmetric lipase dimer operates independently. Bulky compounds such as KET and TET inhibit lipase activity via π-π interactions, primarily targeting the lid domain. In contrast, smaller ligands BRA and HEM exhibit unique binding modes: BRA mirrors TET by localizing near the lid domain, while HEM shows dual interactions with both the lid and catalytic sites. These results underscore the potential of BRA and HEM as promising anti-acne agents, indicating that C. sappan could be an effective herbal remedy for acne. This study provides a foundation for further exploration of natural products in combating acne and mitigating antimicrobial resistance.

Background The similarly in plant physiology and the difficulty of plant classification, in some medicinal plant species, especially plants of the Zingiberaceae family, are a major problem for pharmacologists, leading to mistaken use. To overcome this problem, the proteomic base method was used to study protein profiles of the plant model, Curcuma comosa Roxb., which is a member of the Zingiberaceae and has been used in traditional Thai medicine as an anti-inflammatory agent for the treatment of postpartum uterine bleeding. Results Due to the complexity of protein extraction from this plant, microscale solution-phase isoelectric focusing (MicroSol-IEF) was used to enrich and improve the separation of Curcuma comosa rhizomes phenol-soluble proteins, prior to resolving and analyzing by two-dimensional polyacrylamide gel electrophoresis and identification by tandem mass spectrometry. The protein patterns showed a high abundance of protein spots in the acidic range, including three lectin proteins. The metabolic and defense enzymes, such as superoxide dismutase (SOD) and ascorbate peroxidase, that are associated with antioxidant activity, were mainly found in the basic region. Furthermore, cysteine protease was found in this plant, as had been previously reported in other Zingiberaceae plants. Conclusion This report presents the protein profiles of the ginger plant, Curcuma comosa. Several interesting proteins were identified in this plant that may be used as a protein marker and aid in identifying plants of the Zingiberaceae family.

The objective of this study was to investigate a new protein with α-glucosidase inhibitory activity from the rhizomes of Zingiber ottensii . With a simple salting-out technique followed by single-step anion-exchange purification, the protein was successfully purified from the rhizomes. This protein was found to have three likely sub-unit types, 32.5, 15.2, and 13.8 kDa, as revealed by native and reducing SDS-PAGE analysis. Determination of the kinetics of the inhibition of α-glucosidase from Saccharomyces cerevisiae by standard enzymatic methods indicated the maximum percent inhibition; IC 50 and K i of this protein were 77.5%, 30.15 μg/ml, and 140 μmol, while the K m and V max were 2.35 μmol and 0.11 mM/min, respectively. The inhibitory action was pH-independent within the pH range 2–10, but was potentially affected by buffer salts, and was relatively temperature-stable between 4–35 °C, with a maximum activity at 65 °C. The amino acid sequence of an internal fragment of this purified Z. ottensii rhizomal protein had a similarity to the sequence from the plant cysteine proteinase family. Although this α-glucosidase inhibitory protein was purified from Z. ottensii rhizomes and preliminarily characterized, further studies are needed prior to firm applications being envisaged.

The objective of this study was to investigate a new protein with [alpha]-glucosidase inhibitory activity from the rhizomes of Zingiber ottensii. With a simple salting-out technique followed by single-step anion-exchange purification, the protein was successfully purified from the rhizomes. This protein was found to have three likely sub-unit types, 32.5, 15.2, and 13.8 kDa, as revealed by native and reducing SDS-PAGE analysis. Determination of the kinetics of the inhibition of [alpha]-glucosidase from Saccharomyces cerevisiae by standard enzymatic methods indicated the maximum percent inhibition; IC^sub 50^ and K^sub ^sub i^^ of this protein were 77.5%, 30.15 mcg/ml, and 140 mmol, while the K^sub ^sub m^^ and V^sub ^sub max^^ were 2.35 mmol and 0.11 mM/min, respectively. The inhibitory action was pH-independent within the pH range 2-10, but was potentially affected by buffer salts, and was relatively temperature-stable between 4-35 degrees C, with a maximum activity at 65 degrees C. The amino acid sequence of an internal fragment of this purified Z. ottensii rhizomal protein had a similarity to the sequence from the plant cysteine proteinase family. Although this α-glucosidase inhibitory protein was purified from Z. ottensii rhizomes and preliminarily characterized, further studies are needed prior to firm applications being envisaged. [PUBLICATION ABSTRACT]