Structural studies of metalloporphyrins. Part XI: Complexes of water-soluble zinc(II) porphyrins with amino acids: Influence of ligand-ligand interactions on the stability of the complexes

Determination of l‐theanine in tea water using fluorescence‐visualized paper‐based sensors based on CdTe quantum dots/corn carbon dots and nano‐porphyrin with chemometrics

“…2(D)). The agglomeration rates of metal porphyrins decreased after nano‐crystallization, which increased the probability that the spatial coordination of metal‐acetamido between ZnTPyP and l ‐theanine 48–50 . l ‐theanine (1.0 μmol/L) was added to the quenched CdTe QDs/corn CDs and nano ZnTPyP system, and the fluorescence intensity returned to 72.23% of the original intensity.…”

Comparison of Nonmetal and Metal Hydrophilic Photosensitizer, ATX-S10 (Na) and ATN-2, Binding with Human Serum Proteins Using Spectrophotometry¶

“…One relates to the increased p electron orbitals at the periphery of the porphyrin when the tetrapyrrolic macrocycle associates with adjacent aromatic ligands via ionic binding and van der Waals forces (12). These aromatic ligands are included in amino acids such as phenylalanine, tyrosine and tryptophan, which are contained in serum proteins (15). The induction of a bathochromic shift from the formation of a porphyrin-protein complex is well documented: Hp, one of the components of Photofrin, causes bathochromic shifts when it forms complexes with LDL, HDL (16), albumin or hemopexin (17).…”

“…Lipoproteins are high-molecular weight particles in which a surface layer of apoprotein and amphiphilic lipid molecules encapsulates a nonpolar core of triglyceride and esterified cholesterol molecules (16). The amphiphilic photosensitizer Hp shows the same bathochromic shift of 35 nm with both LDL and HDL (15) and binds to both the apoprotein and lipid moiety of LDL (23). In contrast, the hydrophobic photosensitizer zinc phthalocyanine binds to the lipid core of LDL (23).…”

Comparison of Nonmetal and Metal Hydrophilic Photosensitizer, ATX‐S10 (Na) and ATN‐2, Binding with Human Serum Proteins Using Spectrophotometry¶

“…One relates to the increased χ electron orbitals at the periphery of the porphyrin when the tetrapyrrolic macrocycle associates with adjacent aromatic ligands via ionic binding and van der Waals forces (12). These aromatic ligands are included in amino acids such as phenylalanine, tyrosine and tryptophan, which are contained in serum proteins (15). The induction of a bathochromic shift from the formation of a porphyrin‐protein complex is well documented: Hp, one of the components of Photofrin, causes bathochromic shifts when it forms complexes with LDL, HDL (16), albumin or hemopexin (17).…”