NCNicolás Caicedo

Nicolás Caicedo

*This is an algorithmically generated author record based on publicly available information.

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Nicolás Caicedo has a total of 5 co-authors. Here are the top co-authors by number of shared publications:


Latest Publications

  • Open Access

    Unlocking New Bioactive Peptides from Coffee Pulp: A Metagenomics and AI-Driven Discovery Paradigm

    by Yamil Liscano, Nicolás Caicedo, Jose Oñate-Garzón

    This perspective reframes Colombian coffee pulp from an environmental liability into a strategic asset by proposing a new discovery paradigm. We argue that the pulp’s challenging chemical environment is not a barrier but its key advantage, having acted as a natural evolutionary filter that has sculpted a unique, highly resilient microbiome. Our vision is a technology pipeline that harnesses this natural pre-selection. By converging deep metagenomic data from the pulp’s microbiome with generative artificial intelligence, we can create and validate novel, high-performance bioactive peptides and enzymes that are already pre-optimized for industrial robustness. This approach transcends traditional waste valorization, establishing a new framework for “biointelligence” in action. It offers a strategic roadmap for Colombia to generate knowledge-intensive value chains from its most iconic agricultural product, turning a national challenge into a global opportunity in the bioeconomy.


  • Open Access

    Bioactive Peptides from Quinoa (Chenopodium quinoa Willd.) as Modulators of the Gut Microbiome: A Scoping Review of Preclinical Evidence

    by Nicolás Caicedo, Yamil Liscano, Jose Oñate-Garzón

    Background: Gut microbiome dysbiosis is implicated in numerous chronic diseases. While quinoa possesses a rich nutritional profile with prebiotic potential, the specific capacity of its bioactive peptides to modulate gut microbial communities is not well understood. This scoping review systematically maps the preclinical evidence on the gut microbiome modulatory effects of quinoa-derived bioactive peptides to identify mechanisms, characterize their therapeutic potential, and guide future clinical translation. Methods: Following PRISMA-ScR guidelines, we searched six databases for preclinical studies investigating quinoa-derived peptides or hydrolysates and their effects on gut microbiota. Results: From 834 records, 19 studies met the inclusion criteria. Quinoa interventions demonstrated consistent effects, with 83% of studies reporting enhancement of beneficial genera and 67% an increase in alpha diversity. Disease-specific microbial signatures were observed; for instance, obesity models showed a reduced Firmicutes/Bacteroidetes ratio, while colitis models exhibited decreased Proteobacteria. Butyrate production was consistently enhanced. Methodologically, peptide generation has evolved from traditional fermentation toward more efficient enzymatic hydrolysis. Conclusions: Preclinical evidence strongly suggests that quinoa-derived bioactive peptides act as robust, context-dependent modulators of the gut microbiome. These findings position quinoa as a promising functional ingredient for precision gut health interventions, though clinical translation requires standardized preparations and validation in human trials.


  • Open Access

    Anti-Aging Potential of Bioactive Peptides Derived from Casein Hydrolyzed with Kiwi Actinidin: Integration of In Silico and In Vitro Study

    by Nicolas Caicedo, Lady L. Gamboa, Yhors Ciro, Constain H. Salamanca, Jose Oñate-Garzón

    Background: Skin aging is mainly associated with oxidative stress and enzymatic degradation of collagen and elastin by protease activity. Peptides have antioxidant capacity and inhibitory effects on protease enzymes. Objective: The purpose of this study was to obtain peptides with in vitro anti-aging activity from the enzymatic hydrolysis of bovine casein with actinidin, a protease extracted from the green kiwi fruit (Actinidia deliciosa) Methodology: The enzyme actinidin was extracted from the pulp of the kiwi fruit, purified by ion exchange chromatography and characterized by polyacrylamide electrophoresis (SDS-PAGE). Subsequently, the extracted enzyme was used to hydrolyze commercial bovine casein at 37 °C for 30 min, precipitating the peptide fraction with trichloroacetic acid (TCA), and centrifuged. To determine the anti-aging potential of the peptides in vitro, antioxidant activity was evaluated using the ABTS (2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)) radical. Additionally, the inhibitory capacity of the peptides against collagenase and elastase enzymes was also studied. To complement the in vitro results, the enzymatic hydrolysis of casein with actinidin was simulated. The binding energy (ΔG) of each of the hydrolysates with the collagenase and elastase enzymes was calculated using molecular docking to predict the peptide sequences with the highest probability of interaction. Results: Actinidin was extracted and purified exhibiting a molecular weight close to 27 kDa. The enzyme hydrolyzed the substrate by 91.6%, and the resulting hydrolysates showed moderate in vitro anti-aging activity: antioxidant (17.5%), anticollagenase (18.55%), and antielastase (28.6%). In silico results revealed 66 peptide sequences of which 30.3% consisted of 4–8 amino acids, a suitable size to facilitate interaction with structural targets. The sequences with the highest affinity were FALPQYLK and VIPYVRYL for collagenase and elastase, respectively. Conclusions: Despite the modest inhibition values, the use of a fruit-derived enzyme and a food-grade substrate is in line with current trends in sustainable and natural cosmetics. These findings highlight the great potential for laying the groundwork for future research into actinidin-derived peptides as multifunctional and eco-conscious ingredients for the development of next-generation anti-aging formulations.