Preformulation Studies with Phenylalanine Ammonia Lyase: Essential Prelude to a Microcapsule Formulation for the Management of Phenylketonuria
[Display omitted] . Phenylalanine ammonia lyase (PAL) metabolizes phenylalanine to transcinnamic acid (TCA). Our eventual goal is to develop a PAL microcapsule formulation to deplete phenylalanine in the gastrointestinal tract (g.i.t). The focus of this research is pre-formulation studies with PAL....
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| Published in | Journal of pharmaceutical sciences Vol. 111; no. 7; pp. 1857 - 1867 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
01.07.2022
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| Abstract | [Display omitted] .
Phenylalanine ammonia lyase (PAL) metabolizes phenylalanine to transcinnamic acid (TCA). Our eventual goal is to develop a PAL microcapsule formulation to deplete phenylalanine in the gastrointestinal tract (g.i.t). The focus of this research is pre-formulation studies with PAL. PAL exhibited undesirable time dependent decrease in activity due to TCA mediated product inhibition. Addition of bovine serum albumin (BSA) completely relieved product inhibition. Ultrafiltration experiments revealed that BSA acted by binding and sequestering TCA. PAL exhibits maximum activity at a pH of 8.5 and will need to be buffered to retain activity in the g.i.t. Buffer studies showed that a pH 8.5, 0.4 M Bicine buffer containing BSA was able to maintain maximal PAL activity against simulated gastric and intestinal fluid additions. Buffered PAL with BSA was able to rapidly and completely deplete phenylalanine in simulated mouse g.i.t conditions. A small fraction of phenylalanine in the g.i.t is present as dipeptides. Our studies established for the first time that PAL cannot metabolize phenylalanine dipeptides. Our results explain why previous trials with PAL in the management of phenylketonuria produced low efficacy. They will guide design of a PAL microcapsule formulation that maintains maximal PAL activity during its transit through the g.i.t. |
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| AbstractList | [Display omitted] .
Phenylalanine ammonia lyase (PAL) metabolizes phenylalanine to transcinnamic acid (TCA). Our eventual goal is to develop a PAL microcapsule formulation to deplete phenylalanine in the gastrointestinal tract (g.i.t). The focus of this research is pre-formulation studies with PAL. PAL exhibited undesirable time dependent decrease in activity due to TCA mediated product inhibition. Addition of bovine serum albumin (BSA) completely relieved product inhibition. Ultrafiltration experiments revealed that BSA acted by binding and sequestering TCA. PAL exhibits maximum activity at a pH of 8.5 and will need to be buffered to retain activity in the g.i.t. Buffer studies showed that a pH 8.5, 0.4 M Bicine buffer containing BSA was able to maintain maximal PAL activity against simulated gastric and intestinal fluid additions. Buffered PAL with BSA was able to rapidly and completely deplete phenylalanine in simulated mouse g.i.t conditions. A small fraction of phenylalanine in the g.i.t is present as dipeptides. Our studies established for the first time that PAL cannot metabolize phenylalanine dipeptides. Our results explain why previous trials with PAL in the management of phenylketonuria produced low efficacy. They will guide design of a PAL microcapsule formulation that maintains maximal PAL activity during its transit through the g.i.t. Phenylalanine ammonia lyase (PAL) metabolizes phenylalanine to transcinnamic acid (TCA). Our eventual goal is to develop a PAL microcapsule formulation to deplete phenylalanine in the gastrointestinal tract (g.i.t). The focus of this research is pre-formulation studies with PAL. PAL exhibited undesirable time dependent decrease in activity due to TCA mediated product inhibition. Addition of bovine serum albumin (BSA) completely relieved product inhibition. Ultrafiltration experiments revealed that BSA acted by binding and sequestering TCA. PAL exhibits maximum activity at a pH of 8.5 and will need to be buffered to retain activity in the g.i.t. Buffer studies showed that a pH 8.5, 0.4 M Bicine buffer containing BSA was able to maintain maximal PAL activity against simulated gastric and intestinal fluid additions. Buffered PAL with BSA was able to rapidly and completely deplete phenylalanine in simulated mouse g.i.t conditions. A small fraction of phenylalanine in the g.i.t is present as dipeptides. Our studies established for the first time that PAL cannot metabolize phenylalanine dipeptides. Our results explain why previous trials with PAL in the management of phenylketonuria produced low efficacy. They will guide design of a PAL microcapsule formulation that maintains maximal PAL activity during its transit through the g.i.t. |
| Author | Hakami, Abrar Truong, Nhu Besada, Christina Yetsko, Kyle Dmello, Anil Little, Timothy Pantano, Sharon Pillai, Gayatri |
| Author_xml | – sequence: 1 givenname: Christina orcidid: 0000-0002-1287-2194 surname: Besada fullname: Besada, Christina – sequence: 2 givenname: Abrar surname: Hakami fullname: Hakami, Abrar – sequence: 3 givenname: Gayatri surname: Pillai fullname: Pillai, Gayatri – sequence: 4 givenname: Kyle surname: Yetsko fullname: Yetsko, Kyle – sequence: 5 givenname: Nhu orcidid: 0000-0002-9562-1939 surname: Truong fullname: Truong, Nhu – sequence: 6 givenname: Timothy surname: Little fullname: Little, Timothy – sequence: 7 givenname: Sharon surname: Pantano fullname: Pantano, Sharon – sequence: 8 givenname: Anil orcidid: 0000-0001-8298-387X surname: Dmello fullname: Dmello, Anil email: a.dmello@usciences.edu |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35351497$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1208_s12249_022_02446_y crossref_primary_10_1016_j_ymgmr_2023_101012 crossref_primary_10_1007_s13205_023_03871_x |
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| Keywords | Km Stability Vmax Albumin g.i.t Gastrointestinal tract Phe BH4 BSA TCA PAH Preformulation Microencapsulation PAL PKU Enzyme kinetics Protein formulation HPLC Protein binding |
| Language | English |
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Phenylalanine ammonia lyase (PAL) metabolizes phenylalanine to transcinnamic acid (TCA). Our eventual goal is to develop a PAL microcapsule... Phenylalanine ammonia lyase (PAL) metabolizes phenylalanine to transcinnamic acid (TCA). Our eventual goal is to develop a PAL microcapsule formulation to... |
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| SubjectTerms | Albumin Enzyme kinetics Gastrointestinal tract HPLC Microencapsulation Preformulation Protein binding Protein formulation Stability |
| Title | Preformulation Studies with Phenylalanine Ammonia Lyase: Essential Prelude to a Microcapsule Formulation for the Management of Phenylketonuria |
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