Development and characterization of fused human arginase I for cancer therapy
Recombinant human arginase I (rhArg I) have emerged as a potential candidate for the treatment of varied pathophysiological conditions ranging from arginine-auxotrophic cancer, inflammatory conditions and microbial infection. However, rhArg I have a low circulatory half-life, leading to poor pharmac...
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| Published in: | Investigational new drugs Vol. 41; no. 5; pp. 652 - 663 |
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| Main Authors: | , , , , , |
| Format: | Journal Article |
| Language: | English |
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01-10-2023
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| Abstract | Recombinant human arginase I (rhArg I) have emerged as a potential candidate for the treatment of varied pathophysiological conditions ranging from arginine-auxotrophic cancer, inflammatory conditions and microbial infection. However, rhArg I have a low circulatory half-life, leading to poor pharmacokinetic and pharmacodynamic properties, which necessitating the rapid development of modifications to circumvent these limitations. To address this, polyethylene glycol (PEG)ylated-rhArg I variants are being developed by pharmaceutical companies. However, because of the limitations associated with the clinical use of PEGylated proteins, there is a dire need in the art to develop rhArg I variant(s) which is safe (devoid of limitations of PEGylated counterpart) and possess increased circulatory half-life. In this study, we described the generation and characterization of a fused human arginase I variant (FHA-3) having improved circulatory half-life. FHA-3 protein was engineered by fusing rhArg I with a half-life extension partner (domain of human serum albumin) via a peptide linker and was produced using
P. pastoris
expression system. This purified biopharmaceutical (FHA-3) exhibits (i) increased arginine-hydrolyzing activity in buffer, (ii) cofactor - independency, (iii) increased circulatory half-life (t
1/2
) and (iv) potent anti-cancer activity against human cancer cell lines under in vitro and in vivo conditions. |
|---|---|
| AbstractList | Recombinant human arginase I (rhArg I) have emerged as a potential candidate for the treatment of varied pathophysiological conditions ranging from arginine-auxotrophic cancer, inflammatory conditions and microbial infection. However, rhArg I have a low circulatory half-life, leading to poor pharmacokinetic and pharmacodynamic properties, which necessitating the rapid development of modifications to circumvent these limitations. To address this, polyethylene glycol (PEG)ylated-rhArg I variants are being developed by pharmaceutical companies. However, because of the limitations associated with the clinical use of PEGylated proteins, there is a dire need in the art to develop rhArg I variant(s) which is safe (devoid of limitations of PEGylated counterpart) and possess increased circulatory half-life. In this study, we described the generation and characterization of a fused human arginase I variant (FHA-3) having improved circulatory half-life. FHA-3 protein was engineered by fusing rhArg I with a half-life extension partner (domain of human serum albumin) via a peptide linker and was produced using P. pastoris expression system. This purified biopharmaceutical (FHA-3) exhibits (i) increased arginine-hydrolyzing activity in buffer, (ii) cofactor - independency, (iii) increased circulatory half-life (t1/2) and (iv) potent anti-cancer activity against human cancer cell lines under in vitro and in vivo conditions. Recombinant human arginase I (rhArg I) have emerged as a potential candidate for the treatment of varied pathophysiological conditions ranging from arginine-auxotrophic cancer, inflammatory conditions and microbial infection. However, rhArg I have a low circulatory half-life, leading to poor pharmacokinetic and pharmacodynamic properties, which necessitating the rapid development of modifications to circumvent these limitations. To address this, polyethylene glycol (PEG)ylated-rhArg I variants are being developed by pharmaceutical companies. However, because of the limitations associated with the clinical use of PEGylated proteins, there is a dire need in the art to develop rhArg I variant(s) which is safe (devoid of limitations of PEGylated counterpart) and possess increased circulatory half-life. In this study, we described the generation and characterization of a fused human arginase I variant (FHA-3) having improved circulatory half-life. FHA-3 protein was engineered by fusing rhArg I with a half-life extension partner (domain of human serum albumin) via a peptide linker and was produced using P. pastoris expression system. This purified biopharmaceutical (FHA-3) exhibits (i) increased arginine-hydrolyzing activity in buffer, (ii) cofactor - independency, (iii) increased circulatory half-life (t ) and (iv) potent anti-cancer activity against human cancer cell lines under in vitro and in vivo conditions. Recombinant human arginase I (rhArg I) have emerged as a potential candidate for the treatment of varied pathophysiological conditions ranging from arginine-auxotrophic cancer, inflammatory conditions and microbial infection. However, rhArg I have a low circulatory half-life, leading to poor pharmacokinetic and pharmacodynamic properties, which necessitating the rapid development of modifications to circumvent these limitations. To address this, polyethylene glycol (PEG)ylated-rhArg I variants are being developed by pharmaceutical companies. However, because of the limitations associated with the clinical use of PEGylated proteins, there is a dire need in the art to develop rhArg I variant(s) which is safe (devoid of limitations of PEGylated counterpart) and possess increased circulatory half-life. In this study, we described the generation and characterization of a fused human arginase I variant (FHA-3) having improved circulatory half-life. FHA-3 protein was engineered by fusing rhArg I with a half-life extension partner (domain of human serum albumin) via a peptide linker and was produced using P. pastoris expression system. This purified biopharmaceutical (FHA-3) exhibits (i) increased arginine-hydrolyzing activity in buffer, (ii) cofactor - independency, (iii) increased circulatory half-life (t 1/2 ) and (iv) potent anti-cancer activity against human cancer cell lines under in vitro and in vivo conditions. |
| Author | Pande, Abhay H. Sharma, Nisha Tikoo, Kulbhushan Jawalekar, Snehal Sainath Anakha, J Kawathe, Priyanka Sugriv |
| Author_xml | – sequence: 1 givenname: Snehal Sainath surname: Jawalekar fullname: Jawalekar, Snehal Sainath organization: Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER) – sequence: 2 givenname: Priyanka Sugriv surname: Kawathe fullname: Kawathe, Priyanka Sugriv organization: Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER) – sequence: 3 givenname: Nisha surname: Sharma fullname: Sharma, Nisha organization: Laboratory of Epigenetics and Diseases, Department of Pharmacology and Toxicology, National Institute of Pharmaceutical Education and Research (NIPER) – sequence: 4 givenname: J surname: Anakha fullname: Anakha, J organization: Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER) – sequence: 5 givenname: Kulbhushan surname: Tikoo fullname: Tikoo, Kulbhushan organization: Laboratory of Epigenetics and Diseases, Department of Pharmacology and Toxicology, National Institute of Pharmaceutical Education and Research (NIPER) – sequence: 6 givenname: Abhay H. surname: Pande fullname: Pande, Abhay H. email: apande@niper.ac.in, abbupande@yahoo.co.in organization: Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER) |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/37532976$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1016_j_drudis_2024_103940 |
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| Keywords | Human arginase I Auxotrophy Fusion protein technology Cancer |
| Language | English |
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| SubjectTerms | Anticancer properties Antitumor activity Arginase Cancer Cancer therapies Half-life Human serum albumin Inflammation Life extension Medicine Medicine & Public Health Microorganisms Oncology Pharmaceutical industry Pharmaceuticals Pharmacodynamics Pharmacokinetics Pharmacology/Toxicology Polyethylene glycol Proteins Serum albumin Tumor cell lines |
| Title | Development and characterization of fused human arginase I for cancer therapy |
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