Contact: info@alspinc.com



Dedicated to Developing Effective Therapeutics to Treat Neurodegenerative Disease

 

To Learn More about Research in 

Neurodegenerative Disorders, Please Visit 

 

Alzheimer's Disease: Alzheimer Research Forum

 

Huntington's Disease:

CHDI Foundation Inc.

 

Huntington's Disease Society of America

 

Parkinson's Disease:

Michael J. Fox Foundation

 

Parkinson's Action

 

Traumatic Brain Injury: traumaticbraininjury.com

Beyond innovative technology, our drug discovery process is structured to streamline and expedite the drug development process through leveraging the extensive experience of the team and the multi-indication applications of our compounds. From concept-to-development, approval and beyond - our systematic approach is geared toward moving potential drugs for traumatic brain injury (TBI), Alzheimer's disease (AD) and other neurodegenerative diseases from the laboratory to market as quickly and efficiently as possible.

 

Our Mission


Our Company is striving to develop ground-breaking therapeutics that are directed toward newly-identified causative targets, such as cysteine proteases. By employing a virtual business model, we will recruit the best business, scientific and clinical resources available and motivate them to tackle this challenge with an urgent and unified effort and an eye toward minimizing costs, sharing risk, and vigorously protecting and defending our intellectual property. By maintaining a commitment to honesty, openness, and a dedication to the highest standards obtainable, we can be confident in our expectation that we will be successful in bringing value to the patient, their care givers, and ultimately to the nation and the world.

Background: ALSP’s strategy to combat the ravages of neurodegenerative disease is to deploy its proprietary class of compounds to inhibit papain-like cysteine proteases. The Company’s initial focus on AD and TBI is increasingly supported by mounting evidence that two of these cysteine proteases in particular, cathepsin B and calpain-1, when inappropriately expressed, as is the case in both AD and TBI, come together to create a dangerous intersection at which inflammatory, apoptotic, and necrotic pathways are activated. ALSP believes these pathways constitute the underlying pathology of neurodegeneration.
Consequently, the efficient reversal of the over expression of these two key enzymes can completely mitigate all of these pathways at once and prevent the neuronal destruction that they mediate.  Doing so significantly improves measures of memory deficit and neuro-motor dysfunction in AD and TBI animal models, respectively.  The inhibition of these proteases, not only reduces neurotoxic amyloid-β (Aβ) and neuro-inflammation, but also provides potent neuronal protection by multiple mechanisms. Moreover, this is the only approach we are aware of that has been shown to reduce both full-length Aβ and pyro-glutamate-modified Aβ, the particularly pernicious species implicated to cause AD. Data from AD and TBI models using cathepsin B knock-out animals indicate that this protease plays a dominant role at this intersection and confirms that its inhibition will not have undesired consequences.
Lead Compound: Cathepsin B and calpain-1 activity are significantly elevated in AD and TBI. Both enzymes have been well studied with respect to their contribution to pathways leading to caspase activation and programmed cell death (apoptosis) of the neuron, to inflammatory pathways that include TNF-a, Il-1β and metallo-proteinase activation, and to tissue necrosis.  ALSP’s lead compound, ALP-496, is an orally bio-available, potent inhibitor of both cathepsin B and calpain-1 that efficiently crosses the blood brain barrier (BBB) and is not a substrate for the P-gp pump that reverses BBB penetration. Elimination of the drug is primarily through the kidney and the gut without multi-dosing accumulation.  Extensive work with ALP-496-related tool compounds has established that this class of compounds has a wide therapeutic window and that they are well tolerated by humans even after extended periods of dosing.
Background: ALSP’s strategy to combat the ravages of neurodegenerative disease is to deploy its proprietary class of compounds to inhibit papain-like cysteine proteases. The Company’s initial focus on AD and TBI is increasingly supported by mounting evidence that two of these cysteine proteases in particular, cathepsin B and calpain-1, when inappropriately expressed, as is the case in both AD and TBI, come together to create a dangerous intersection at which inflammatory, apoptotic, and necrotic pathways are activated. ALSP believes these pathways constitute the underlying pathology of neurodegeneration.
Consequently, the efficient reversal of the over expression of these two key enzymes can completely mitigate all of these pathways at once and prevent the neuronal destruction that they mediate.  Doing so significantly improves measures of memory deficit and neuro-motor dysfunction in AD and TBI animal models, respectively.  The inhibition of these proteases, not only reduces neurotoxic amyloid-β (Aβ) and neuro-inflammation, but also provides potent neuronal protection by multiple mechanisms. Moreover, this is the only approach we are aware of that has been shown to reduce both full-length Aβ and pyro-glutamate-modified Aβ, the particularly pernicious species implicated to cause AD. Data from AD and TBI models using cathepsin B knock-out animals indicate that this protease plays a dominant role at this intersection and confirms that its inhibition will not have undesired consequences.
Lead Compound: Cathepsin B and calpain-1 activity are significantly elevated in AD and TBI. Both enzymes have been well studied with respect to their contribution to pathways leading to caspase activation and programmed cell death (apoptosis) of the neuron, to inflammatory pathways that include TNF-a, Il-1β and metallo-proteinase activation, and to tissue necrosis.  ALSP’s lead compound, ALP-496, is an orally bio-available, potent inhibitor of both cathepsin B and calpain-1 that efficiently crosses the blood brain barrier (BBB) and is not a substrate for the P-gp pump that reverses BBB penetration. Elimination of the drug is primarily through the kidney and the gut without multi-dosing accumulation.  Extensive work with ALP-496-related tool compounds has established that this class of compounds has a wide therapeutic window and that they are well tolerated by humans even after extended periods of dosing.
Background: ALSP’s strategy to combat the ravages of neurodegenerative disease is to deploy its proprietary class of compounds to inhibit papain-like cysteine proteases. The Company’s initial focus on traumatic brain injury (TBI) and Alzheimer's disease (AD) is increasingly supported by mounting evidence that two of these cysteine proteases in particular, cathepsin B and calpain-1, when inappropriately expressed, as is the case in both traumatic brain injury (TBI) and Alzheimer's disease (AD), come together to create a dangerous intersection at which inflammatory, apoptotic, and necrotic pathways are activated. ALSP believes these pathways constitute the underlying pathology of neurodegeneration.

Consequently, the efficient reversal of the over expression of these two key enzymes can completely mitigate all of these pathways at once and prevent the neuronal destruction that they mediate.  Doing so significantly improves measures of memory deficit and neuro-motor dysfunction in AD and TBI animal models, respectively.  The inhibition of these proteases, not only reduces neurotoxic amyloid-β (Aβ) and neuro-inflammation, but also provides potent neuronal protection by multiple mechanisms. Moreover, this is the only approach we are aware of that has been shown to reduce both full-length Aβ and pyro-glutamate-modified Aβ, the particularly pernicious species implicated to cause AD. Data from AD and TBI models using cathepsin B knock-out animals indicate that this protease plays a dominant role at this intersection and confirms that its inhibition will not have undesired consequences.
Consequently, the efficient reversal of the over expression of these two key enzymes can completely mitigate all of these pathways at once and prevent the neuronal destruction that they mediate.  Doing so significantly improves measures of memory deficit and neuro-motor dysfunction in AD and TBI animal models, respectively.  The inhibition of these proteases, not only reduces neurotoxic amyloid-β (Aβ) and neuro-inflammation, but also provides potent neuronal protection by multiple mechanisms. Moreover, this is the only approach we are aware of that has been shown to reduce both full-length Aβ and pyro-glutamate-modified Aβ, the particularly pernicious species implicated to cause AD. Data from AD and TBI models using cathepsin B knock-out animals indicate that this protease plays a dominant role at this intersection and confirms that its inhibition will not have undesired consequences.
Consequently, the efficient reversal of the over expression of these two key enzymes can completely mitigate all of these pathways at once and prevent the neuronal destruction that they mediate.  Doing so significantly improves measures of memory deficit and neuro-motor dysfunction in TBI and AD animal models, respectively.  The inhibition of these proteases, not only reduces neurotoxic amyloid-β (Aβ) and neuro-inflammation, but also provides potent neuronal protection by multiple mechanisms. Moreover, this is the only approach we are aware of that has been shown to reduce both full-length Aβ and pyro-glutamate-modified Aβ, the particularly pernicious species implicated to cause AD. Data from TBI and AD models using cathepsin B knock-out animals indicate that this protease plays a dominant role at this intersection and confirms that its inhibition will not have undesired consequences.

Consequently, the efficient reversal of the over expression of these two key enzymes can completely mitigate all of these pathways at once and prevent the neuronal destruction that they mediate.  Doing so significantly improves measures of memory deficit and neuro-motor dysfunction in AD and TBI animal models, respectively.  The inhibition of these proteases, not only reduces neurotoxic amyloid-β (Aβ) and neuro-inflammation, but also provides potent neuronal protection by multiple mechanisms. Moreover, this is the only approach we are aware of that has been shown to reduce both full-length Aβ and pyro-glutamate-modified Aβ, the particularly pernicious species implicated to cause AD. Data from AD and TBI models using cathepsin B knock-out animals indicate that this protease plays a dominant role at this intersection and confirms that its inhibition will not have undesired consequences.
Lead Compound: Cathepsin B and calpain-1 activity are significantly elevated in AD and TBI. Both enzymes have been well studied with respect to their contribution to pathways leading to caspase activation and programmed cell death (apoptosis) of the neuron, to inflammatory pathways that include TNF-a, Il-1β and metallo-proteinase activation, and to tissue necrosis.  ALSP’s lead compound, ALP-496, is an orally bio-available, potent inhibitor of both cathepsin B and calpain-1 that efficiently crosses the blood brain barrier (BBB) and is not a substrate for the P-gp pump that reverses BBB penetration. Elimination of the drug is primarily through the kidney and the gut without multi-dosing accumulation.  Extensive work with ALP-496-related tool compounds has established that this class of compounds has a wide therapeutic window and that they are well tolerated by humans even after extended periods of dosing
Consequently, the efficient reversal of the over expression of these two key enzymes can completely mitigate all of these pathways at once and prevent the neuronal destruction that they mediate.  Doing so significantly improves measures of memory deficit and neuro-motor dysfunction in AD and TBI animal models, respectively.  The inhibition of these proteases, not only reduces neurotoxic amyloid-β (Aβ) and neuro-inflammation, but also provides potent neuronal protection by multiple mechanisms. Moreover, this is the only approach we are aware of that has been shown to reduce both full-length Aβ and pyro-glutamate-modified Aβ, the particularly pernicious species implicated to cause AD. Data from AD and TBI models using cathepsin B knock-out animals indicate that this protease plays a dominant role at this intersection and confirms that its inhibition will not have undesired consequences.
Lead Compound: Cathepsin B and calpain-1 activity are significantly elevated in AD and TBI. Both enzymes have been well studied with respect to their contribution to pathways leading to caspase activation and programmed cell death (apoptosis) of the neuron, to inflammatory pathways that include TNF-a, Il-1β and metallo-proteinase activation, and to tissue necrosis.  ALSP’s lead compound, ALP-496, is an orally bio-available, potent inhibitor of both cathepsin B and calpain-1 that efficiently crosses the blood brain barrier (BBB) and is not a substrate for the P-gp pump that reverses BBB penetration. Elimination of the drug is primarily through the kidney and the gut without multi-dosing accumulation.  Extensive work with ALP-496-related tool compounds has established that this class of compounds has a wide therapeutic window and that they are well tolerated by humans even after extended periods of dosing
Consequently, the efficient reversal of the over expression of these two key enzymes can completely mitigate all of these pathways at once and prevent the neuronal destruction that they mediate.  Doing so significantly improves measures of memory deficit and neuro-motor dysfunction in AD and TBI animal models, respectively.  The inhibition of these proteases, not only reduces neurotoxic amyloid-β (Aβ) and neuro-inflammation, but also provides potent neuronal protection by multiple mechanisms. Moreover, this is the only approach we are aware of that has been shown to reduce both full-length Aβ and pyro-glutamate-modified Aβ, the particularly pernicious species implicated to cause AD. Data from AD and TBI models using cathepsin B knock-out animals indicate that this protease plays a dominant role at this intersection and confirms that its inhibition will not have undesired consequences.
Consequently, the efficient reversal of the over expression of these two key enzymes can completely mitigate all of these pathways at once and prevent the neuronal destruction that they mediate.  Doing so significantly improves measures of memory deficit and neuro-motor dysfunction in AD and TBI animal models, respectively.  The inhibition of these proteases, not only reduces neurotoxic amyloid-β (Aβ) and neuro-inflammation, but also provides potent neuronal protection by multiple mechanisms. Moreover, this is the only approach we are aware of that has been shown to reduce both full-length Aβ and pyro-glutamate-modified Aβ, the particularly pernicious species implicated to cause AD. Data from AD and TBI models using cathepsin B knock-out animals indicate that this protease plays a dominant role at this intersection and confirms that its inhibition will not have undesired consequences.
Lead Compound: Cathepsin B and calpain-1 activity are significantly elevated in TBI and AD. Both enzymes have been well studied with respect to their contribution to pathways leading to caspase activation and programmed cell death (apoptosis) of the neuron, to inflammatory pathways that include TNF-a, Il-1β and metallo-proteinase activation, and to tissue necrosis.  ALSP’s lead compound, ALP-496, is an orally bio-available, potent inhibitor of both cathepsin B and calpain-1 that efficiently crosses the blood brain barrier (BBB) and is not a substrate for the P-gp pump that reverses BBB penetration. Elimination of the drug is primarily through the kidney and the gut without multi-dosing accumulation.  Extensive work with ALP-496-related tool compounds has established that this class of compounds has a wide therapeutic window and that they are well tolerated by humans even after extended periods of dosing.
Consequently, the efficient reversal of the over expression of these two key enzymes can completely mitigate all of these pathways at once and prevent the neuronal destruction that they mediate.  Doing so significantly improves measures of memory deficit and neuro-motor dysfunction in AD and TBI animal models, respectively.  The inhibition of these proteases, not only reduces neurotoxic amyloid-β (Aβ) and neuro-inflammation, but also provides potent neuronal protection by multiple mechanisms. Moreover, this is the only approach we are aware of that has been shown to reduce both full-length Aβ and pyro-glutamate-modified Aβ, the particularly pernicious species implicated to cause AD. Data from AD and TBI models using cathepsin B knock-out animals indicate that this protease plays a dominant role at this intersection and confirms that its inhibition will not have undesired consequences.
Lead Compound: Cathepsin B and calpain-1 activity are significantly elevated in AD and TBI. Both enzymes have been well studied with respect to their contribution to pathways leading to caspase activation and programmed cell death (apoptosis) of the neuron, to inflammatory pathways that include TNF-a, Il-1β and metallo-proteinase activation, and to tissue necrosis.  ALSP’s lead compound, ALP-496, is an orally bio-available, potent inhibitor of both cathepsin B and calpain-1 that efficiently crosses the blood brain barrier (BBB) and is not a substrate for the P-gp pump that reverses BBB penetration. Elimination of the drug is primarily through the kidney and the gut without multi-dosing accumulation.  Extensive work with ALP-496-related tool compounds has established that this class of compounds has a wide therapeutic window and that they are well tolerated by humans even after extended periods of dosing