Literature DB >> 33805682

Study of the l-Phenylalanine Ammonia-Lyase Penetration Kinetics and the Efficacy of Phenylalanine Catabolism Correction Using In Vitro Model Systems.

Lyubov Dyshlyuk1,2, Stanislav Sukhikh2,3, Svetlana Noskova3, Svetlana Ivanova1,4, Alexander Prosekov5, Olga Babich3.   

Abstract

The kinetics of l-phenylalanine ammonia-lyase (PAL) penetration into the monolayer of liver cells after its release from capsules was studied. The studies showed the absence of the effect of the capsule shell based on plant hydrocolloids on the absorption of l-phenylalanine ammonia-lyase in systems simulating the liver surface. After 120 min of incubation, in all variants of the experiment, from 87.0 to 96.8% of the enzyme penetrates the monolayer of liver cells. The combined analysis of the results concludes that the developed encapsulated form of l-phenylalanine ammonia-lyase is characterized by high efficiency in correcting the disturbed catabolism of phenylalanine in phenylketonuria, which is confirmed by the results of experiments carried out on in vitro model systems. PAL is approved for the treatment of adult patients with phenylketonuria. The encapsulated l-phenylalanine ammonia-lyase form can find therapeutic application in the phenylketonuria treatment after additional in vitro and in vivo studies, in particular, the study of preparation safety indicators. Furthermore, it demonstrated high efficacy in tumor regression and the treatment of tyrosine-related metabolic disorders such as tyrosinemia. Several therapeutically valuable metabolites biosynthesized by PAL via its catalytic action are included in food supplements, antimicrobial peptides, drugs, amino acids, and their derivatives. PAL, with improved pharmacodynamic and pharmacokinetic properties, is a highly effective medical drug.

Entities:  

Keywords:  biomedical drug; catabolism disorder; enzyme; kinetics; l-phenylalanine ammonia-lyase; phenylketonuria

Year:  2021        PMID: 33805682      PMCID: PMC7999051          DOI: 10.3390/pharmaceutics13030383

Source DB:  PubMed          Journal:  Pharmaceutics        ISSN: 1999-4923            Impact factor:   6.321


  23 in total

1.  Six phenylalanine ammonia-lyases from Camellia sinensis: Evolution, expression, and kinetics.

Authors:  Yingling Wu; Wenzhao Wang; Yanzhi Li; Xinlong Dai; Guoliang Ma; Dawei Xing; Mengqing Zhu; Liping Gao; Tao Xia
Journal:  Plant Physiol Biochem       Date:  2017-06-29       Impact factor: 4.270

Review 2.  Phenylalanine ammonia lyase (PAL): From discovery to enzyme substitution therapy for phenylketonuria.

Authors:  Harvey L Levy; Christineh N Sarkissian; Charles R Scriver
Journal:  Mol Genet Metab       Date:  2018-06-09       Impact factor: 4.797

3.  Large neutral amino acids block phenylalanine transport into brain tissue in patients with phenylketonuria.

Authors:  J Pietz; R Kreis; A Rupp; E Mayatepek; D Rating; C Boesch; H J Bremer
Journal:  J Clin Invest       Date:  1999-04       Impact factor: 14.808

Review 4.  Psychosocial aspects of PKU: hidden disabilities--a review.

Authors:  J K Gentile; A E Ten Hoedt; A M Bosch
Journal:  Mol Genet Metab       Date:  2010       Impact factor: 4.797

5.  A survey of natural protein intake in Dutch phenylketonuria patients: insight into estimation or measurement of dietary intake.

Authors:  Margreet van Rijn; Jolanda Jansma; Aeltsje Brinksma; H D Bakker; G H J Boers; E Carbasius-Weber; A C Douwes; A van den Herberg; N M Ter Horst; J B C de Klerk; T J de Koning; L van den Ploeg; M E Rubio-Gozalbo; J P Sels; R C A Sengers; H W de Valk; H Termeulen; H Zweers; Francjan J van Spronsen
Journal:  J Am Diet Assoc       Date:  2008-10

6.  Biochemical Evaluation of Phenylalanine Ammonia Lyase from Endemic Plant Cyathobasis fruticulosa (Bunge) Aellen. for the Dietary Treatment of Phenylketonuria.

Authors:  Seda Şirin; Selcen Babaoğlu Aydaş; Belma Aslım
Journal:  Food Technol Biotechnol       Date:  2016-09       Impact factor: 3.918

7.  Exploring the therapeutic potential of modern and ancestral phenylalanine/tyrosine ammonia-lyases as supplementary treatment of hereditary tyrosinemia.

Authors:  Natalie M Hendrikse; Albin Holmberg Larsson; Stefan Svensson Gelius; Sergei Kuprin; Erik Nordling; Per-Olof Syrén
Journal:  Sci Rep       Date:  2020-01-28       Impact factor: 4.379

8.  Study of the Potential of the Capsule Shell Based on Natural Polysaccharides in Targeted Delivery of the L-Phenylalanine Ammonia-Lyase Enzyme Preparation.

Authors:  Olga Babich; Lyubov Dyshlyuk; Alexander Prosekov; Svetlana Noskova; Oksana Ivina; Valery Pavsky; Svetlana Ivanova; Olga Bulgakova
Journal:  Pharmaceuticals (Basel)       Date:  2020-04-09

9.  Saturation Mutagenesis for Phenylalanine Ammonia Lyases of Enhanced Catalytic Properties.

Authors:  Raluca Bianca Tomoiagă; Souad Diana Tork; Ilka Horváth; Alina Filip; Levente Csaba Nagy; László Csaba Bencze
Journal:  Biomolecules       Date:  2020-05-30

10.  The production of L- and D-phenylalanines using engineered phenylalanine ammonia lyases from Petroselinum crispum.

Authors:  Souad Diana Tork; Emma Zsófia Aletta Nagy; Lilla Cserepes; Diana Monica Bordea; Botond Nagy; Monica Ioana Toşa; Csaba Paizs; László Csaba Bencze
Journal:  Sci Rep       Date:  2019-12-27       Impact factor: 4.379

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