Adamax

Kolbaev SN, Sharonova IN, Skrebitsky VG

Bulletin of Experimental Biology and Medicine

In rat hippocampal and cerebellar brain slices, the parent peptide Semax increased the frequency of spontaneous intracellular calcium fluctuations in hippocampal CA1 pyramidal neurons without affecting proton-stimulated calcium entry in cerebellar granule cells, helping localize the cellular targets relevant to its neuroprotective mechanism. (ADAMAX is an adamantane/acetyl-modified Semax analogue; this study characterizes the parent peptide.)

Sudarkina OY, Filippenkov IB, Stavchansky VV, Denisova AE, Yuzhakov VV, Sevan’kaeva LE, et al.

International Journal of Molecular Sciences

In a rat transient middle-cerebral-artery-occlusion model, the parent peptide Semax modulated brain protein expression — upregulating active CREB and downregulating MMP-9, c-Fos, and active JNK — consistent with suppression of inflammatory and cell-death pathways and activation of recovery signaling. (Characterizes the parent peptide Semax; ADAMAX is a modified analogue.)

Magrì A, Tabbì G, Giuffrida A, Pappalardo G, Satriano C, Naletova I, et al.

Journal of Inorganic Biochemistry

This inorganic-biochemistry study characterized N-terminally acetylated Semax (Ac-Semax) — the acetylation modification ADAMAX shares — showing that acetylation alters the peptide’s copper(II)/zinc(II) coordination chemistry and redox behavior relative to unmodified Semax, and examined the metal-complex effects in SH-SY5Y neuroblastoma cell culture. Does not address ADAMAX’s adamantane modification.

Shevchenko KV, Nagaev IY, Andreeva LA, Shevchenko VP, Myasoedov NF

Doklady Biological Sciences

This study measured the proteolytic stability of acetylated Semax against aminopeptidase degradation in rat brain- and blood-derived biological media relative to unmodified Semax, characterizing how N-terminal acetylation — one of ADAMAX’s two modifications — affects a Semax-class peptide’s enzymatic breakdown. Does not address ADAMAX’s adamantane modification.

Dolotov OV, Karpenko EA, Seredenina TS, Inozemtseva LS, Levitskaya NG, Zolotarev YA, et al.

Journal of Neurochemistry

In rat basal forebrain, the parent peptide Semax showed specific, reversible, calcium-dependent membrane binding sites (dissociation constant ~2.4 nM) and, after intranasal application, a rapid increase in brain-derived neurotrophic factor (BDNF) protein levels, supporting a neurotrophic-pathway mechanism. (Characterizes the parent peptide Semax.)

Eremin KO, Kudrin VS, Saransaari P, Oja SS, Grivennikov IA, Myasoedov NF, et al.

Neurochemical Research

In rodents, the parent peptide Semax modulated striatal serotonergic activity (increasing 5-HIAA) and enhanced amphetamine-evoked striatal dopamine release and locomotor activity, indicating positive modulation of monoaminergic systems linked to its nootropic profile. (Characterizes the parent peptide Semax.)