Augusto Zuluaga-Vélez

Dr. Augusto Zuluaga-Vélez

Medicine, Technological University of Pereira, Pereira, Risaralda, Colombia
orcid

Research Focus & Metrics

Academic Career Length

8Years (2019-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 September 2021 in Biomedicine & Pharmacotherapy
Verified
Journal Article
Open access
AZAugusto Zuluaga-Vélez
Augusto Zuluaga-Vélez
AQAdrián Quintero-Martinez
Adrián Quintero-Martinez
LOLina M. Orozco
Lina M. Orozco
JSJuan Carlos Sepúlveda-Arias
Juan Carlos Sepúlveda-Arias
Silk fibroin is a protein with intrinsic characteristics that make it a good candidate as a scaffold for tissue engineering. Recent works have enhanced its benefits by adding inorganic phases that interact with silk fibroin in different ways. A systematic review was performed in four databases to study the physicochemical and biological performance of silk fibroin nanocomposites. In the last decade, only 51 articles contained either in vitro cell culture models or in vivo tests. The analysis of such works resulted in their classification into the following scaffold types: particles, mats and textiles, films, hydrogels, sponge-like structures, and mixed conformations. From the physicochemical perspective, the inorganic phase imbued in silk fibroin nanocomposites resulted in better stability and mechanical performance. This review revealed that the inorganic phase may be associated with specific biological responses, such as neovascularisation, cell differentiation, cell proliferation, and antimicrobial and immunomodulatory activity. The study of nanocomposites as tissue engineering scaffolds is a highly active area mostly focused on bone and cartilage regeneration with promising results. Nonetheless, there are still many challenges related to their application in other tissues, a better understanding of the interaction between the inorganic and organic phases, and the associated biological response.

4 March 2019 in PLOS ONE
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Journal Article
Open access
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AZAugusto Zuluaga-Vélez
Augusto Zuluaga-Vélez
DCDiego Fernando Cómbita-Merchán
Diego Fernando Cómbita-Merchán
Robison BuitragoRobison Buitrago
Robison Buitrago
JSJuan Felipe Santa
Juan Felipe Santa
EAEnrique Aguilar-Fernández
Enrique Aguilar-Fernández
JSJuan Carlos Sepúlveda-Arias
Juan Carlos Sepúlveda-Arias
Hydrogel scaffolds are important materials in tissue engineering, and their characterization is essential to determine potential biomedical applications according to their mechanical and structural behavior. In this work, silk fibroin hydrogels were synthesized by two different methods (vortex and sonication), and agarose hydrogels were also obtained for comparison purposes. Samples were characterized by scanning electron microscopy, infrared analysis, thermo-gravimetrical analysis, confined compression test, and rheological test. The results indicate that nanofibers can be obtained via both silk fibroin and agarose hydrogels. The mechanical tests showed that the Young’s modulus is similar to those found in the literature, with the highest value for agarose hydrogels. All the hydrogels showed a shear-thinning behavior. Additionally, the MTT test revealed that silk fibroin hydrogels had low cytotoxicity in THP-1 and HEK-293 cells, whereas the agarose hydrogels showed high toxicity for the THP-1 cell line. The results indicate that silk fibroin hydrogels obtained from a Colombian silkworm hybrid are suitable for the development of scaffolds, with potential applications in tissue engineering.

26 January 2024 in European Journal of Pharmaceutical Sciences
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Journal Article
Open access
DGDavid González-Restrepo
David González-Restrepo
AZAugusto Zuluaga-Vélez
Augusto Zuluaga-Vélez
LOLina M. Orozco
Lina M. Orozco
JSJuan Carlos Sepúlveda-Arias
Juan Carlos Sepúlveda-Arias
Silk fibroin is a fibrillar protein obtained from arthropods such as mulberry and non-mulberry silkworms. Silk fibroin has been used as a dressing in wound treatment for its physical, chemical, mechanical, and biological properties. This systematic review analyzed studies from PubMed, Web of Science, and Scopus databases to identify the molecules preferred for functionalizing silk fibroin-based dressings and to describe their mechanisms of exhibiting anti-inflammatory and antibacterial properties. The analysis of the selected articles allowed us to classify the dressings into different conformations, such as membranes, films, hydrogels, sponges, and bioadhesives. The incorporation of various molecules, including antibiotics, natural products, peptides, nanocomposites, nanoparticles, secondary metabolites, growth factors, and cytokines, has allowed the development of dressings that promote wound healing with antibacterial and immunomodulatory properties. In addition, silk fibroin-based dressings have been established to have the potential to regenerate wounds such as venous ulcers, arterial ulcers, diabetic foot, third-degree burns, and neoplastic ulcers. Evaluation of the efficacy of silk fibroin-based dressings in tissue engineering is an area of great activity that has shown significant advances in recent years.

25 February 2024 in Methods and Protocols
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JMJhon Jairo Melchor-Moncada
Jhon Jairo Melchor-Moncada
AGAlejandra García-Barco
Alejandra García-Barco
AZAugusto Zuluaga-Vélez
Augusto Zuluaga-Vélez
LVLuz Angela Veloza
Luz Angela Veloza
JSJuan Carlos Sepúlveda-Arias
Juan Carlos Sepúlveda-Arias
Serratiopeptidase, a bacterial metalloprotease known for its pain-relieving and anti-inflammatory properties, can be produced through fermentation with S. marcescens. This study aimed to identify key factors related to nutrient composition and physicochemical conditions for production in Erlenmeyer flasks and to scale up the mixture to a bioreactor to obtain the maximum proteolytic activity. A Plackett–Burman design was used to determine whether the presence of silkworm pupae (at 1.5%) was a significant parameter for serratiopeptidase production. Along with the variables pH, temperature, and time, they were optimized using a Taguchi experimental design, resulting in values of 7, 25 °C, and 36 h, respectively. Scaling up with a kLa of 25.45 ± 3.12 h−1 showed the highest serratiopeptidase production at 24 h. A factorial design was used for ultrafiltration, resulting in an LMH (liters per square meter per hour) of 960 L/m2h, a TMP (transmembrane pressure) of 15 psi, and a concentration factor of five, with a specific activity of 24,325.81 ± 1515.69 U/mg. Afterward, the retentate was purified using strong anion exchange chromatography and ultrafiltration, yielding a 19.94 ± 3.07% recovery and a purification factor of 1.59 ± 0.31. In conclusion, waste from the sericulture industry can be used for serratiopeptidase production.

13 August 2022 in Heliyon
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Journal Article
Open access
MCMaría C. Cardona-Trujillo
María C. Cardona-Trujillo
TOTatiana Ocampo-Cárdenas
Tatiana Ocampo-Cárdenas
FTFredy A. Tabares-Villa
Fredy A. Tabares-Villa
AZAugusto Zuluaga-Vélez
Augusto Zuluaga-Vélez
JSJuan Carlos Sepúlveda-Arias
Juan Carlos Sepúlveda-Arias
Zika virus (ZIKV) and Chikungunya virus (CHIKV) are arboviruses that cause important viral diseases affecting the world population. Both viruses can produce remarkably similar clinical manifestations, co-circulate in a geographic region, and coinfections have been documented, thus making clinical diagnosis challenging. Therefore, it is urgent to have better molecular techniques that allow a differential, sensitive and rapid diagnosis from body fluid samples. This systematic review explores evidence in the literature regarding the advances in the molecular diagnosis of Zika and Chikungunya in humans, published from 2010 to March 2021. Four databases were consulted (Scopus, PubMed, Web of Science, and Embase) and a total of 31 studies were included according to the selection criteria. Our analysis highlights the need for standardization in the report and interpretation of new promising diagnostic methods. It also examines the benefits of new alternatives for the molecular diagnosis of these arboviruses, in contrast to established methods.

Verified
Journal Article
Open access
PDF file
JMJhon Jairo Melchor-Moncada
Jhon Jairo Melchor-Moncada
SVSantiago Vasquez-Giraldo
Santiago Vasquez-Giraldo
AZAugusto Zuluaga-Vélez
Augusto Zuluaga-Vélez
LALina Marcela Orozco Arboleda
Lina Marcela Orozco Arboleda
LVLuz Angela Veloza
Luz Angela Veloza
JSJuan Carlos Sepúlveda-Arias
Juan Carlos Sepúlveda-Arias
Antimicrobial resistance (AMR) poses a significant global health threat, necessitating the development of novel antibacterial strategies. Serratiopeptidase (SP), a metalloprotease produced by bacteria such as Serratia marcescens, has gained attention not only for its anti-inflammatory properties but also for its potential antibacterial activity. However, its protein nature makes it susceptible to pH changes and self-proteolysis, limiting its effectiveness. This study aimed to increase both the enzymatic stability and antibacterial activity of serratiopeptidase through immobilization on titanium oxide nanoparticles (TiO2-NPs), leveraging the biocompatibility and stability of these nanomaterials. Commercial TiO2-NPs were characterized using TGA/DTG, FT-IR, UV–Vis, and XRD analyses, and their biocompatibility was assessed through cytotoxicity studies. Serratiopeptidase was produced via fermentation using the C8 isolate of Serratia marcescens obtained from the intestine of Bombyx mori L., purified chromatographically, and immobilized on carboxylated nanoparticles via EDC/NHS coupling at various pH conditions. The optimal enzymatic activity was achieved by using pH 5.1 for nanoparticle activation and pH 5.5 for enzyme coupling. The resulting bioconjugate demonstrated stable proteolytic activity at 25 °C for 48 h. Immobilization was confirmed by FT-IR spectroscopy, and the Michaelis–Menten kinetics were determined. Notably, the bioconjugate exhibited two-fold greater antibacterial activity against E. coli than the free enzyme or TiO2-NPs at 1000 µg/mL. This study successfully developed a serratiopeptidase–TiO2 bioconjugate with enhanced enzymatic stability and antibacterial properties. The improved antibacterial activity of the immobilized enzyme presents a promising approach for developing new tools to combat antimicrobial resistance, with potential applications in healthcare, food safety, and environmental protection.