LHRH, also named gonadotropin-releasing hormone (GnRH), is an endogenous peptide agonist (primary sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) released from hypothalamus. LHRH-R (LHRH receptor), a member of the G protein-coupled receptor family, is overexpressed in various tumor types, while their expression in the corresponding normal tissues, apart from pituitary cells, is comparatively low. Given this, we chose LHRH as the TTP component of MSCPTP (TTP-CPP peptide). In this investigation, we combined LHRH (as the TTP part), peptide PLGLAG, T2 (as the CPP part) and cysteine (as linker binding site) into an MSCPTP named LT-1. Then PTX was conjugated with LT-1 via a GSH-cleavable module to produce the smart PDC, namely LTP-1 (TTP-CPP-PTX conjugate). In vitro, LTP-1 exhibited selective and stronger cytotoxicity than PTX against LHRH-R-positive tumor cells with little effect on normal cells. In vivo, LTP-1 was highly effective in suppressing tumor growth in an MCF-7 xenograft mouse model. Additional experiments on both cellular and molecular levels were carried out to unravel the possible antitumor mechanism of action of LTP-1.

LHRH, also named gonadotropin-releasing hormone (GnRH), is an endogenous peptide agonist (primary sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) released from hypothalamus. LHRH-R (LHRH receptor), a member of the G protein-coupled receptor family, is overexpressed in various tumor types, while their expression in the corresponding normal tissues, apart from pituitary cells, is comparatively low. Given this, we chose LHRH as the TTP component of MSCPTP (TTP-CPP peptide). In this investigation, we combined LHRH (as the TTP part), peptide PLGLAG, T2 (as the CPP part) and cysteine (as linker binding site) into an MSCPTP named LT-1. Then PTX was conjugated with LT-1 via a GSH-cleavable module to produce the smart PDC, namely LTP-1 (TTP-CPP-PTX conjugate). In vitro, LTP-1 exhibited selective and stronger cytotoxicity than PTX against LHRH-R-positive tumor cells with little effect on normal cells. In vivo, LTP-1 was highly effective in suppressing tumor growth in an MCF-7 xenograft mouse model. Additional experiments on both cellular and molecular levels were carried out to unravel the possible antitumor mechanism of action of LTP-1.

LHRH, also named gonadotropin-releasing hormone (GnRH), is an endogenous peptide agonist (primary sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) released from hypothalamus. LHRH-R (LHRH receptor), a member of the G protein-coupled receptor family, is overexpressed in various tumor types, while their expression in the corresponding normal tissues, apart from pituitary cells, is comparatively low. Given this, we chose LHRH as the TTP component of MSCPTP (TTP-CPP peptide). In this investigation, we combined LHRH (as the TTP part), peptide PLGLAG, T2 (as the CPP part) and cysteine (as linker binding site) into an MSCPTP named LT-1. Then PTX was conjugated with LT-1 via a GSH-cleavable module to produce the smart PDC, namely LTP-1 (TTP-CPP-PTX conjugate). In vitro, LTP-1 exhibited selective and stronger cytotoxicity than PTX against LHRH-R-positive tumor cells with little effect on normal cells. In vivo, LTP-1 was highly effective in suppressing tumor growth in an MCF-7 xenograft mouse model. Additional experiments on both cellular and molecular levels were carried out to unravel the possible antitumor mechanism of action of LTP-1.

LHRH, also named gonadotropin-releasing hormone (GnRH), is an endogenous peptide agonist (primary sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) released from hypothalamus. LHRH-R (LHRH receptor), a member of the G protein-coupled receptor family, is overexpressed in various tumor types, while their expression in the corresponding normal tissues, apart from pituitary cells, is comparatively low. Given this, we chose LHRH as the TTP component of MSCPTP (TTP-CPP peptide). In this investigation, we combined LHRH (as the TTP part), peptide PLGLAG, T2 (as the CPP part) and cysteine (as linker binding site) into an MSCPTP named LT-1. Then PTX was conjugated with LT-1 via a GSH-cleavable module to produce the smart PDC, namely LTP-1 (TTP-CPP-PTX conjugate). In vitro, LTP-1 exhibited selective and stronger cytotoxicity than PTX against LHRH-R-positive tumor cells with little effect on normal cells. In vivo, LTP-1 was highly effective in suppressing tumor growth in an MCF-7 xenograft mouse model. Additional experiments on both cellular and molecular levels were carried out to unravel the possible antitumor mechanism of action of LTP-1.

LHRH, also named gonadotropin-releasing hormone (GnRH), is an endogenous peptide agonist (primary sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) released from hypothalamus. LHRH-R (LHRH receptor), a member of the G protein-coupled receptor family, is overexpressed in various tumor types, while their expression in the corresponding normal tissues, apart from pituitary cells, is comparatively low. Given this, we chose LHRH as the TTP component of MSCPTP (TTP-CPP peptide). In this investigation, we combined LHRH (as the TTP part), peptide PLGLAG, T2 (as the CPP part) and cysteine (as linker binding site) into an MSCPTP named LT-1. Then PTX was conjugated with LT-1 via a GSH-cleavable module to produce the smart PDC, namely LTP-1 (TTP-CPP-PTX conjugate). In vitro, LTP-1 exhibited selective and stronger cytotoxicity than PTX against LHRH-R-positive tumor cells with little effect on normal cells. In vivo, LTP-1 was highly effective in suppressing tumor growth in an MCF-7 xenograft mouse model. Additional experiments on both cellular and molecular levels were carried out to unravel the possible antitumor mechanism of action of LTP-1.

LHRH, also named gonadotropin-releasing hormone (GnRH), is an endogenous peptide agonist (primary sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) released from hypothalamus. LHRH-R (LHRH receptor), a member of the G protein-coupled receptor family, is overexpressed in various tumor types, while their expression in the corresponding normal tissues, apart from pituitary cells, is comparatively low. Given this, we chose LHRH as the TTP component of MSCPTP (TTP-CPP peptide). In this investigation, we combined LHRH (as the TTP part), peptide PLGLAG, T2 (as the CPP part) and cysteine (as linker binding site) into an MSCPTP named LT-1. Then PTX was conjugated with LT-1 via a GSH-cleavable module to produce the smart PDC, namely LTP-1 (TTP-CPP-PTX conjugate). In vitro, LTP-1 exhibited selective and stronger cytotoxicity than PTX against LHRH-R-positive tumor cells with little effect on normal cells. In vivo, LTP-1 was highly effective in suppressing tumor growth in an MCF-7 xenograft mouse model. Additional experiments on both cellular and molecular levels were carried out to unravel the possible antitumor mechanism of action of LTP-1.

LHRH, also named gonadotropin-releasing hormone (GnRH), is an endogenous peptide agonist (primary sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) released from hypothalamus. LHRH-R (LHRH receptor), a member of the G protein-coupled receptor family, is overexpressed in various tumor types, while their expression in the corresponding normal tissues, apart from pituitary cells, is comparatively low. Given this, we chose LHRH as the TTP component of MSCPTP (TTP-CPP peptide). In this investigation, we combined LHRH (as the TTP part), peptide PLGLAG, T2 (as the CPP part) and cysteine (as linker binding site) into an MSCPTP named LT-1. Then PTX was conjugated with LT-1 via a GSH-cleavable module to produce the smart PDC, namely LTP-1 (TTP-CPP-PTX conjugate). In vitro, LTP-1 exhibited selective and stronger cytotoxicity than PTX against LHRH-R-positive tumor cells with little effect on normal cells. In vivo, LTP-1 was highly effective in suppressing tumor growth in an MCF-7 xenograft mouse model. Additional experiments on both cellular and molecular levels were carried out to unravel the possible antitumor mechanism of action of LTP-1.

LHRH, also named gonadotropin-releasing hormone (GnRH), is an endogenous peptide agonist (primary sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) released from hypothalamus. LHRH-R (LHRH receptor), a member of the G protein-coupled receptor family, is overexpressed in various tumor types, while their expression in the corresponding normal tissues, apart from pituitary cells, is comparatively low. Given this, we chose LHRH as the TTP component of MSCPTP (TTP-CPP peptide). In this investigation, we combined LHRH (as the TTP part), peptide PLGLAG, T2 (as the CPP part) and cysteine (as linker binding site) into an MSCPTP named LT-1. Then PTX was conjugated with LT-1 via a GSH-cleavable module to produce the smart PDC, namely LTP-1 (TTP-CPP-PTX conjugate). In vitro, LTP-1 exhibited selective and stronger cytotoxicity than PTX against LHRH-R-positive tumor cells with little effect on normal cells. In vivo, LTP-1 was highly effective in suppressing tumor growth in an MCF-7 xenograft mouse model. Additional experiments on both cellular and molecular levels were carried out to unravel the possible antitumor mechanism of action of LTP-1.

LHRH, also named gonadotropin-releasing hormone (GnRH), is an endogenous peptide agonist (primary sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) released from hypothalamus. LHRH-R (LHRH receptor), a member of the G protein-coupled receptor family, is overexpressed in various tumor types, while their expression in the corresponding normal tissues, apart from pituitary cells, is comparatively low. Given this, we chose LHRH as the TTP component of MSCPTP (TTP-CPP peptide). In this investigation, we combined LHRH (as the TTP part), peptide PLGLAG, T2 (as the CPP part) and cysteine (as linker binding site) into an MSCPTP named LT-1. Then PTX was conjugated with LT-1 via a GSH-cleavable module to produce the smart PDC, namely LTP-1 (TTP-CPP-PTX conjugate). In vitro, LTP-1 exhibited selective and stronger cytotoxicity than PTX against LHRH-R-positive tumor cells with little effect on normal cells. In vivo, LTP-1 was highly effective in suppressing tumor growth in an MCF-7 xenograft mouse model. Additional experiments on both cellular and molecular levels were carried out to unravel the possible antitumor mechanism of action of LTP-1.

LHRH, also named gonadotropin-releasing hormone (GnRH), is an endogenous peptide agonist (primary sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) released from hypothalamus. LHRH-R (LHRH receptor), a member of the G protein-coupled receptor family, is overexpressed in various tumor types, while their expression in the corresponding normal tissues, apart from pituitary cells, is comparatively low. Given this, we chose LHRH as the TTP component of MSCPTP (TTP-CPP peptide). In this investigation, we combined LHRH (as the TTP part), peptide PLGLAG, T2 (as the CPP part) and cysteine (as linker binding site) into an MSCPTP named LT-1. Then PTX was conjugated with LT-1 via a GSH-cleavable module to produce the smart PDC, namely LTP-1 (TTP-CPP-PTX conjugate). In vitro, LTP-1 exhibited selective and stronger cytotoxicity than PTX against LHRH-R-positive tumor cells with little effect on normal cells. In vivo, LTP-1 was highly effective in suppressing tumor growth in an MCF-7 xenograft mouse model. Additional experiments on both cellular and molecular levels were carried out to unravel the possible antitumor mechanism of action of LTP-1.

LHRH, also named gonadotropin-releasing hormone (GnRH), is an endogenous peptide agonist (primary sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) released from hypothalamus. LHRH-R (LHRH receptor), a member of the G protein-coupled receptor family, is overexpressed in various tumor types, while their expression in the corresponding normal tissues, apart from pituitary cells, is comparatively low. Given this, we chose LHRH as the TTP component of MSCPTP (TTP-CPP peptide). In this investigation, we combined LHRH (as the TTP part), peptide PLGLAG, T2 (as the CPP part) and cysteine (as linker binding site) into an MSCPTP named LT-1. Then PTX was conjugated with LT-1 via a GSH-cleavable module to produce the smart PDC, namely LTP-1 (TTP-CPP-PTX conjugate). In vitro, LTP-1 exhibited selective and stronger cytotoxicity than PTX against LHRH-R-positive tumor cells with little effect on normal cells. In vivo, LTP-1 was highly effective in suppressing tumor growth in an MCF-7 xenograft mouse model. Additional experiments on both cellular and molecular levels were carried out to unravel the possible antitumor mechanism of action of LTP-1.