Selectivein vivo tumor localization of heptacar☐ylic porphyrin isomer I in a bladder tumor model: a novel technique to modulate porphyrin localization

Thermodynamics of porphyrin binding to human serum albumin using affinity capillary electrophoresis

“…This combination allowed a higher fraction of unbound HCP to circulate and accumulate in abnormal tissues. The same explanation was given [5] on the tumor localization ability of HPD, in which the high binding affinity of PP to serum proteins allowed other porphyrin components (e. g., dimers and oligomers) in HPD to circulate "free" (i. e., unbound to various serum proteins), thus enhancing their tumor uptake.…”

“…El-Far and co-workers [5] have examined the tumor localization property of HCP and found that it can be selectively retained in bladder malignant cells. Furthermore, these researchers have found that higher uptake of HCP in the tumor (without prolonged retention in the skin) can be obtained by the addition of another porphyrin with higher binding affinity to serum proteins.…”

“…On the basis of porphyrin-protein binding studies, a number of research groups [4,5] have made an interesting postulation that porphyrins which show poor affinity for circulating serum proteins, such as uroporphyrin (a highly hydrophilic porphyrin containing eight carboxylic groups), are better tumor localization compounds. The polycarboxylated groups in the porphyrin molecule were postulated to be responsible for enhanced tumor affinity when compared to HPD (predominated with hydrophobic porphyrin species containing only two carboxylic groups).…”

Thermodynamics of porphyrin binding to human serum albumin using affinity capillary electrophoresis

“…This combination allowed a higher fraction of unbound HCP to circulate and accumulate in abnormal tissues. The same explanation was given [5] on the tumor localization ability of HPD, in which the high binding affinity of PP to serum proteins allowed other porphyrin components (e. g., dimers and oligomers) in HPD to circulate "free" (i. e., unbound to various serum proteins), thus enhancing their tumor uptake.…”

“…El-Far and co-workers [5] have examined the tumor localization property of HCP and found that it can be selectively retained in bladder malignant cells. Furthermore, these researchers have found that higher uptake of HCP in the tumor (without prolonged retention in the skin) can be obtained by the addition of another porphyrin with higher binding affinity to serum proteins.…”

“…On the basis of porphyrin-protein binding studies, a number of research groups [4,5] have made an interesting postulation that porphyrins which show poor affinity for circulating serum proteins, such as uroporphyrin (a highly hydrophilic porphyrin containing eight carboxylic groups), are better tumor localization compounds. The polycarboxylated groups in the porphyrin molecule were postulated to be responsible for enhanced tumor affinity when compared to HPD (predominated with hydrophobic porphyrin species containing only two carboxylic groups).…”

Recent Developments of Porphyrin Photosensitizers in Photodynamic Therapy

“…Epidermal swelling, redness, and blistering are all signs of the moderate version of the photosensitivity syndrome; however, the severe form may be dangerous [45][46][47][48]. The chemical modification and its purification lead to the development of HpD derivatives, which show high selectivity of tumor tissues and cause less intense skin photosensitivity than the Hp [49][50][51]. The HpD derivatives photofrin compounds, and their targeting ability are listed in Table -1.…”

Binding studies of porphyrins to human serum albumin using affinity capillary electrophoresis

“…It has been postulated that porphyrins with moderate affinity with the carriers (proteins), such as HCP, should possess better tumor localization property [6]. When compared to UP (lower affinity), El-Far and co-workers [11,12] had found that HCP was a better photosensitizer for the selective localization in bladder malignant cells. And interestingly, by introducing another porphyrin with higher binding affinity (e.g., PP) for serum proteins, a higher fraction of unbound HCP appeared to circulate 'free' (i.e., unbound to various serum proteins) in the vicinity of tumor sites and resulting in a higher uptake of HCP by malignant cells [12].…”

Thermodynamics of porphyrin binding to human serum albumin using affinity capillary electrophoresis

“…This combination allowed a higher fraction of unbound HCP to circulate and accumulate in abnormal tissues. The same explanation was given [5] on the tumor localization ability of HPD, in which the high binding affinity of PP to serum proteins allowed other porphyrin components (e. g., dimers and oligomers) in HPD to circulate "free" (i. e., unbound to various serum proteins), thus enhancing their tumor uptake.…”

“…El-Far and co-workers [5] have examined the tumor localization property of HCP and found that it can be selectively retained in bladder malignant cells. Furthermore, these researchers have found that higher uptake of HCP in the tumor (without prolonged retention in the skin) can be obtained by the addition of another porphyrin with higher binding affinity to serum proteins.…”

“…On the basis of porphyrin-protein binding studies, a number of research groups [4,5] have made an interesting postulation that porphyrins which show poor affinity for circulating serum proteins, such as uroporphyrin (a highly hydrophilic porphyrin containing eight carboxylic groups), are better tumor localization compounds. The polycarboxylated groups in the porphyrin molecule were postulated to be responsible for enhanced tumor affinity when compared to HPD (predominated with hydrophobic porphyrin species containing only two carboxylic groups).…”

Recent Developments of Porphyrin Photosensitizers in Photodynamic Therapy

“…Epidermal swelling, redness, and blistering are all signs of the moderate version of the photosensitivity syndrome; however, the severe form may be dangerous [45][46][47][48]. The chemical modification and its purification lead to the development of HpD derivatives, which show high selectivity of tumor tissues and cause less intense skin photosensitivity than the Hp [49][50][51]. The HpD derivatives photofrin compounds, and their targeting ability are listed in Table -1.…”

Binding studies of porphyrins to human serum albumin using affinity capillary electrophoresis

“…It has been postulated that porphyrins with moderate affinity with the carriers (proteins), such as HCP, should possess better tumor localization property [6]. When compared to UP (lower affinity), El-Far and co-workers [11,12] had found that HCP was a better photosensitizer for the selective localization in bladder malignant cells. And interestingly, by introducing another porphyrin with higher binding affinity (e.g., PP) for serum proteins, a higher fraction of unbound HCP appeared to circulate 'free' (i.e., unbound to various serum proteins) in the vicinity of tumor sites and resulting in a higher uptake of HCP by malignant cells [12].…”

Thermodynamics of porphyrin binding to human serum albumin using affinity capillary electrophoresis

“…This combination allowed a higher fraction of unbound HCP to circulate and accumulate in abnormal tissues. The same explanation was given [5] on the tumor localization ability of HPD, in which the high binding affinity of PP to serum proteins allowed other porphyrin components (e. g., dimers and oligomers) in HPD to circulate "free" (i. e., unbound to various serum proteins), thus enhancing their tumor uptake.…”

“…El-Far and co-workers [5] have examined the tumor localization property of HCP and found that it can be selectively retained in bladder malignant cells. Furthermore, these researchers have found that higher uptake of HCP in the tumor (without prolonged retention in the skin) can be obtained by the addition of another porphyrin with higher binding affinity to serum proteins.…”

“…On the basis of porphyrin-protein binding studies, a number of research groups [4,5] have made an interesting postulation that porphyrins which show poor affinity for circulating serum proteins, such as uroporphyrin (a highly hydrophilic porphyrin containing eight carboxylic groups), are better tumor localization compounds. The polycarboxylated groups in the porphyrin molecule were postulated to be responsible for enhanced tumor affinity when compared to HPD (predominated with hydrophobic porphyrin species containing only two carboxylic groups).…”

Recent Developments of Porphyrin Photosensitizers in Photodynamic Therapy

“…Epidermal swelling, redness, and blistering are all signs of the moderate version of the photosensitivity syndrome; however, the severe form may be dangerous [45][46][47][48]. The chemical modification and its purification lead to the development of HpD derivatives, which show high selectivity of tumor tissues and cause less intense skin photosensitivity than the Hp [49][50][51]. The HpD derivatives photofrin compounds, and their targeting ability are listed in Table -1.…”

Binding studies of porphyrins to human serum albumin using affinity capillary electrophoresis

“…It has been postulated that porphyrins with moderate affinity with the carriers (proteins), such as HCP, should possess better tumor localization property [6]. When compared to UP (lower affinity), El-Far and co-workers [11,12] had found that HCP was a better photosensitizer for the selective localization in bladder malignant cells. And interestingly, by introducing another porphyrin with higher binding affinity (e.g., PP) for serum proteins, a higher fraction of unbound HCP appeared to circulate 'free' (i.e., unbound to various serum proteins) in the vicinity of tumor sites and resulting in a higher uptake of HCP by malignant cells [12].…”